CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  BI06  ***

elNémo ID: 221206043343109505

Job options:

ID        	=	 221206043343109505
JOBID     	=	 BI06
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER BI06

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-JUL-14   4QTB              
TITLE     STRUCTURE OF HUMAN ERK1 IN COMPLEX WITH SCH772984 REVEALING A NOVEL   
TITLE    2 INHIBITOR-INDUCED BINDING POCKET                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 3;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: MAP KINASE 3, MAPK 3, ERT2, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   6 KINASE 1, ERK-1, INSULIN-STIMULATED MAP2 KINASE, MAP KINASE ISOFORM  
COMPND   7 P44, P44-MAPK, MICROTUBULE-ASSOCIATED PROTEIN 2 KINASE, P44-ERK1;    
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ERK1, MAPK3, PRKM3;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-R3-PRARE2;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 TRANSFERASE, KINASE, MAPK, SIGNALLING, INHIBITOR, ALLOSTERIC,        
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM (SGC), TRANSFERASE-TRANSFERASE        
KEYWDS   4 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,T.KEATES,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA, 
AUTHOR   2 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
REVDAT   2   24-SEP-14 4QTB    1       JRNL                                     
REVDAT   1   23-JUL-14 4QTB    0                                                
JRNL        AUTH   A.CHAIKUAD,E.M C TACCONI,J.ZIMMER,Y.LIANG,N.S.GRAY,          
JRNL        AUTH 2 M.TARSOUNAS,S.KNAPP                                          
JRNL        TITL   A UNIQUE INHIBITOR BINDING SITE IN ERK1/2 IS ASSOCIATED WITH 
JRNL        TITL 2 SLOW BINDING KINETICS.                                       
JRNL        REF    NAT.CHEM.BIOL.                V.  10   853 2014              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   25195011                                                     
JRNL        DOI    10.1038/NCHEMBIO.1629                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 133341                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7044                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9557                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 500                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 193                                     
REMARK   3   SOLVENT ATOMS            : 1111                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.80                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.86000                                             
REMARK   3    B22 (A**2) : 1.25000                                              
REMARK   3    B33 (A**2) : -0.38000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.07000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.056         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.039         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.892         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.967                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6273 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6104 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8500 ; 1.631 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14079 ; 0.789 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   767 ; 5.695 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   297 ;37.140 ;23.603       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1126 ;11.410 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;18.793 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   921 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7316 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1464 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2880 ; 0.987 ; 0.895       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2879 ; 0.973 ; 0.893       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3619 ; 1.555 ; 1.339       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3619 ; 1.555 ; 1.339       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3393 ; 1.812 ; 1.128       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3393 ; 1.812 ; 1.128       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4848 ; 2.780 ; 1.598       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8320 ; 6.252 ; 9.919       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8318 ; 6.252 ; 9.917       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    24        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8830  46.5650  57.0340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0198 T22:   0.0248                                     
REMARK   3      T33:   0.0384 T12:   0.0037                                     
REMARK   3      T13:  -0.0033 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1775 L22:   0.1231                                     
REMARK   3      L33:   0.2187 L12:  -0.0042                                     
REMARK   3      L13:  -0.0332 L23:  -0.0492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0111 S12:   0.0028 S13:  -0.0202                       
REMARK   3      S21:   0.0009 S22:   0.0165 S23:   0.0054                       
REMARK   3      S31:  -0.0125 S32:  -0.0028 S33:  -0.0054                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   350        A   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.2390  50.0410  49.5610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0226 T22:   0.0367                                     
REMARK   3      T33:   0.0759 T12:  -0.0077                                     
REMARK   3      T13:   0.0032 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3376 L22:   0.7579                                     
REMARK   3      L33:   3.3625 L12:   0.3773                                     
REMARK   3      L13:   0.8165 L23:   0.5347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0505 S12:  -0.0275 S13:  -0.0326                       
REMARK   3      S21:   0.0227 S22:  -0.0423 S23:  -0.1508                       
REMARK   3      S31:   0.0679 S32:  -0.0520 S33:  -0.0081                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    27        B   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5980  30.8560  90.6400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0230 T22:   0.0167                                     
REMARK   3      T33:   0.0398 T12:   0.0061                                     
REMARK   3      T13:   0.0025 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3377 L22:   0.0498                                     
REMARK   3      L33:   0.2393 L12:   0.0235                                     
REMARK   3      L13:   0.0901 L23:   0.0445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:   0.0095 S13:   0.0237                       
REMARK   3      S21:  -0.0069 S22:   0.0105 S23:  -0.0011                       
REMARK   3      S31:  -0.0074 S32:   0.0058 S33:   0.0008                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   350        B   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8320  27.5070  81.8550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0215 T22:   0.0344                                     
REMARK   3      T33:   0.0597 T12:  -0.0069                                     
REMARK   3      T13:   0.0051 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9390 L22:   0.7833                                     
REMARK   3      L33:   3.5242 L12:   0.5810                                     
REMARK   3      L13:  -1.3860 L23:  -0.4425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0624 S12:  -0.0958 S13:   0.0274                       
REMARK   3      S21:   0.0276 S22:  -0.0637 S23:   0.1220                       
REMARK   3      S31:  -0.0583 S32:   0.1075 S33:   0.0013                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4QTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086486.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91997                            
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : KIRKPATRICK BAEZ BIMORPH MIRROR    
REMARK 200                                   PAIR                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140385                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ZOQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% PEG4000, 0.1 M TRIS PH 8.0 AND 0.2   
REMARK 280  M LITHIUM SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  277.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.00500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     LEU A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     ALA A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     ARG B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     VAL B   375                                                      
REMARK 465     LEU B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 465     ALA B   378                                                      
REMARK 465     PRO B   379                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B  27    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   358     O    HOH A  1066              2.06            
REMARK 500   O    HOH A   955     O    HOH A   956              2.10            
REMARK 500   OE1  GLU A   267     O    HOH A   993              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 322   CD    GLU A 322   OE1     0.083                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 141   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG B 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 166       38.56   -147.99                                   
REMARK 500    ASP A 184       87.31     72.12                                   
REMARK 500    ASN A 218       15.77   -163.22                                   
REMARK 500    LEU A 311       46.49   -103.64                                   
REMARK 500    ASP A 335       89.71   -160.81                                   
REMARK 500    ASP B 166       41.62   -152.18                                   
REMARK 500    ASP B 184       86.99     76.01                                   
REMARK 500    ASN B 218       13.44   -161.99                                   
REMARK 500    LEU B 311       35.83    -96.46                                   
REMARK 500    ASP B 335       89.00   -161.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 762        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 851        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A1071        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH B 912        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B 938        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH B 952        DISTANCE =  5.74 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 416                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38Z A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 409                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38Z B 412                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QTA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QTC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QTD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QTE   RELATED DB: PDB                                   
DBREF  4QTB A    1   379  UNP    P27361   MK03_HUMAN       1    379             
DBREF  4QTB B    1   379  UNP    P27361   MK03_HUMAN       1    379             
SEQADV 4QTB SER A    0  UNP  P27361              EXPRESSION TAG                 
SEQADV 4QTB SER B    0  UNP  P27361              EXPRESSION TAG                 
SEQRES   1 A  380  SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY GLY GLY          
SEQRES   2 A  380  GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY VAL PRO          
SEQRES   3 A  380  GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE ASP VAL          
SEQRES   4 A  380  GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY GLU GLY          
SEQRES   5 A  380  ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS VAL ARG          
SEQRES   6 A  380  LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU          
SEQRES   7 A  380  HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE GLN          
SEQRES   8 A  380  ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE GLY ILE          
SEQRES   9 A  380  ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA MET ARG          
SEQRES  10 A  380  ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU          
SEQRES  11 A  380  TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN ASP HIS          
SEQRES  12 A  380  ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS          
SEQRES  13 A  380  TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS          
SEQRES  14 A  380  PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP LEU LYS          
SEQRES  15 A  380  ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP PRO GLU          
SEQRES  16 A  380  HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR          
SEQRES  17 A  380  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS          
SEQRES  18 A  380  GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS          
SEQRES  19 A  380  ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO          
SEQRES  20 A  380  GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY          
SEQRES  21 A  380  ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE          
SEQRES  22 A  380  ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER LEU PRO          
SEQRES  23 A  380  SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE PRO LYS          
SEQRES  24 A  380  SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG MET LEU          
SEQRES  25 A  380  THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU GLU ALA          
SEQRES  26 A  380  LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO THR          
SEQRES  27 A  380  ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE ALA MET          
SEQRES  28 A  380  GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS GLU LEU          
SEQRES  29 A  380  ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY VAL LEU          
SEQRES  30 A  380  GLU ALA PRO                                                  
SEQRES   1 B  380  SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY GLY GLY          
SEQRES   2 B  380  GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY VAL PRO          
SEQRES   3 B  380  GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE ASP VAL          
SEQRES   4 B  380  GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY GLU GLY          
SEQRES   5 B  380  ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS VAL ARG          
SEQRES   6 B  380  LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU          
SEQRES   7 B  380  HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE GLN          
SEQRES   8 B  380  ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE GLY ILE          
SEQRES   9 B  380  ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA MET ARG          
SEQRES  10 B  380  ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU          
SEQRES  11 B  380  TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN ASP HIS          
SEQRES  12 B  380  ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS          
SEQRES  13 B  380  TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS          
SEQRES  14 B  380  PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP LEU LYS          
SEQRES  15 B  380  ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP PRO GLU          
SEQRES  16 B  380  HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR          
SEQRES  17 B  380  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS          
SEQRES  18 B  380  GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS          
SEQRES  19 B  380  ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO          
SEQRES  20 B  380  GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY          
SEQRES  21 B  380  ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE          
SEQRES  22 B  380  ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER LEU PRO          
SEQRES  23 B  380  SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE PRO LYS          
SEQRES  24 B  380  SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG MET LEU          
SEQRES  25 B  380  THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU GLU ALA          
SEQRES  26 B  380  LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO THR          
SEQRES  27 B  380  ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE ALA MET          
SEQRES  28 B  380  GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS GLU LEU          
SEQRES  29 B  380  ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY VAL LEU          
SEQRES  30 B  380  GLU ALA PRO                                                  
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       8                                                       
HET    EDO  A 407       8                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    EDO  A 411       4                                                       
HET    EDO  A 412       4                                                       
HET    EDO  A 413       4                                                       
HET    DMS  A 414       4                                                       
HET    DMS  A 415       4                                                       
HET     CL  A 416       1                                                       
HET    SO4  A 417       5                                                       
HET    38Z  A 418      44                                                       
HET    EDO  B 401       8                                                       
HET    EDO  B 402       4                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    EDO  B 405       4                                                       
HET    EDO  B 406       4                                                       
HET    EDO  B 407       4                                                       
HET    DMS  B 408       4                                                       
HET     CL  B 409       1                                                       
HET     CL  B 410       1                                                       
HET    SO4  B 411       5                                                       
HET    38Z  B 412      44                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     38Z (3R)-1-(2-OXO-2-{4-[4-(PYRIMIDIN-2-YL)PHENYL]PIPERAZIN-          
HETNAM   2 38Z  1-YL}ETHYL)-N-[3-(PYRIDIN-4-YL)-2H-INDAZOL-5-                   
HETNAM   3 38Z  YL]PYRROLIDINE-3-CARBOXAMIDE                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    20(C2 H6 O2)                                                 
FORMUL  16  DMS    3(C2 H6 O S)                                                 
FORMUL  18   CL    3(CL 1-)                                                     
FORMUL  19  SO4    2(O4 S 2-)                                                   
FORMUL  20  38Z    2(C33 H33 N9 O2)                                             
FORMUL  33  HOH   *1111(H2 O)                                                   
HELIX    1   1 HIS A   78  PHE A   95  1                                  18    
HELIX    2   2 LEU A  129  GLN A  136  1                                   8    
HELIX    3   3 SER A  139  ALA A  160  1                                  22    
HELIX    4   4 LYS A  168  SER A  170  5                                   3    
HELIX    5   5 ASP A  192  ASP A  196  5                                   5    
HELIX    6   6 THR A  207  ARG A  211  5                                   5    
HELIX    7   7 ALA A  212  MET A  216  5                                   5    
HELIX    8   8 LYS A  224  ASN A  241  1                                  18    
HELIX    9   9 HIS A  249  GLY A  262  1                                  14    
HELIX   10  10 SER A  265  ASN A  270  1                                   6    
HELIX   11  11 ASN A  274  SER A  283  1                                  10    
HELIX   12  12 ALA A  291  PHE A  296  1                                   6    
HELIX   13  13 ASP A  300  LEU A  311  1                                  12    
HELIX   14  14 ASN A  314  ARG A  318  5                                   5    
HELIX   15  15 THR A  320  ALA A  326  1                                   7    
HELIX   16  16 HIS A  327  GLU A  331  5                                   5    
HELIX   17  17 ASP A  335  GLU A  339  5                                   5    
HELIX   18  18 ALA A  349  LEU A  355  5                                   7    
HELIX   19  19 PRO A  356  ALA A  369  1                                  14    
HELIX   20  20 ARG A  370  GLN A  372  5                                   3    
HELIX   21  21 HIS B   78  PHE B   95  1                                  18    
HELIX   22  22 LEU B  129  GLN B  136  1                                   8    
HELIX   23  23 SER B  139  ALA B  160  1                                  22    
HELIX   24  24 LYS B  168  SER B  170  5                                   3    
HELIX   25  25 ASP B  192  ASP B  196  5                                   5    
HELIX   26  26 THR B  207  ARG B  211  5                                   5    
HELIX   27  27 ALA B  212  MET B  216  5                                   5    
HELIX   28  28 LYS B  224  ASN B  241  1                                  18    
HELIX   29  29 HIS B  249  GLY B  262  1                                  14    
HELIX   30  30 SER B  265  ASN B  270  1                                   6    
HELIX   31  31 ASN B  274  SER B  283  1                                  10    
HELIX   32  32 ALA B  291  PHE B  296  1                                   6    
HELIX   33  33 ASP B  300  LEU B  311  1                                  12    
HELIX   34  34 THR B  320  ALA B  326  1                                   7    
HELIX   35  35 HIS B  327  GLU B  331  5                                   5    
HELIX   36  36 ASP B  335  GLU B  339  5                                   5    
HELIX   37  37 ALA B  349  LEU B  355  5                                   7    
HELIX   38  38 PRO B  356  ALA B  369  1                                  14    
HELIX   39  39 ARG B  370  GLN B  372  5                                   3    
SHEET    1   A 2 GLU A  29  VAL A  31  0                                        
SHEET    2   A 2 GLN A  34  PHE A  36 -1  O  PHE A  36   N  GLU A  29           
SHEET    1   B 5 TYR A  42  GLY A  51  0                                        
SHEET    2   B 5 GLY A  54  ASP A  61 -1  O  TYR A  60   N  THR A  43           
SHEET    3   B 5 THR A  66  ILE A  73 -1  O  THR A  66   N  ASP A  61           
SHEET    4   B 5 VAL A 118  GLN A 122 -1  O  GLN A 122   N  ALA A  69           
SHEET    5   B 5 ASP A 105  LEU A 107 -1  N  ASP A 105   O  VAL A 121           
SHEET    1   C 3 THR A 127  ASP A 128  0                                        
SHEET    2   C 3 LEU A 172  ILE A 174 -1  O  ILE A 174   N  THR A 127           
SHEET    3   C 3 LEU A 180  ILE A 182 -1  O  LYS A 181   N  LEU A 173           
SHEET    1   D 2 VAL A 162  LEU A 163  0                                        
SHEET    2   D 2 ARG A 189  ILE A 190 -1  O  ARG A 189   N  LEU A 163           
SHEET    1   E 2 GLU B  29  VAL B  31  0                                        
SHEET    2   E 2 GLN B  34  PHE B  36 -1  O  GLN B  34   N  VAL B  31           
SHEET    1   F 5 TYR B  42  GLY B  51  0                                        
SHEET    2   F 5 GLY B  54  ASP B  61 -1  O  TYR B  60   N  THR B  43           
SHEET    3   F 5 THR B  66  ILE B  73 -1  O  ILE B  70   N  SER B  57           
SHEET    4   F 5 VAL B 118  GLN B 122 -1  O  GLN B 122   N  ALA B  69           
SHEET    5   F 5 ASP B 105  LEU B 107 -1  N  ASP B 105   O  VAL B 121           
SHEET    1   G 3 THR B 127  ASP B 128  0                                        
SHEET    2   G 3 LEU B 172  ILE B 174 -1  O  ILE B 174   N  THR B 127           
SHEET    3   G 3 LEU B 180  ILE B 182 -1  O  LYS B 181   N  LEU B 173           
SHEET    1   H 2 VAL B 162  LEU B 163  0                                        
SHEET    2   H 2 ARG B 189  ILE B 190 -1  O  ARG B 189   N  LEU B 163           
CISPEP   1 GLY A   39    PRO A   40          0         6.07                     
CISPEP   2 GLN A  372    PRO A  373          0        -5.36                     
CISPEP   3 GLY B   39    PRO B   40          0         5.17                     
CISPEP   4 GLN B  372    PRO B  373          0        -5.80                     
SITE     1 AC1  3 ASP A  37  LEU A 107  HOH A 635                               
SITE     1 AC2  6 GLU A  98  ASN A  99  GLN A 149  ARG A 152                    
SITE     2 AC2  6 ASP A 179  HOH A 576                                          
SITE     1 AC3  4 LEU A 201  GLU A 203  TYR A 250  HOH A1051                    
SITE     1 AC4  8 ARG A  84  ARG A  87  GLY A 186  LEU A 187                    
SITE     2 AC4  8 ALA A 188  ARG A 189  HOH A 704  HOH A 926                    
SITE     1 AC5  4 TYR A 130  SER A 170  EDO A 413  HOH A 733                    
SITE     1 AC6  7 ILE A 190  ALA A 191  THR A 347  PHE A 348                    
SITE     2 AC6  7 ALA A 349  DMS A 415  HOH A 976                               
SITE     1 AC7  7 ASP A 141  TYR A 145  TYR A 333  HOH A 974                    
SITE     2 AC7  7 LYS B 289  VAL B 290  ALA B 291                               
SITE     1 AC8  4 SER A 263  PRO A 285  HOH A 595  HOH A1008                    
SITE     1 AC9  6 SER A 263  LEU A 281  GLN A 282  LEU A 284                    
SITE     2 AC9  6 SER A 286  HOH A 578                                          
SITE     1 BC1  1 GLU A 323                                                     
SITE     1 BC2  5 PRO A  40  ARG A  41  HIS A  62  VAL A  63                    
SITE     2 BC2  5 HOH A 908                                                     
SITE     1 BC3  4 LYS A  65  LEU A 201  TYR A 280  HOH A 911                    
SITE     1 BC4  5 ASP A 128  TYR A 130  EDO A 405  HOH A 685                    
SITE     2 BC4  5 HOH A1026                                                     
SITE     1 BC5  4 LEU A 239  SER A 299  HOH A 541  HOH A 731                    
SITE     1 BC6  7 ARG A 189  ILE A 190  ASP A 192  PHE A 348                    
SITE     2 BC6  7 MET A 350  EDO A 406  HOH A 574                               
SITE     1 BC7  5 HIS A 197  ASN A 218  ILE A 273  ASN A 274                    
SITE     2 BC7  5 ARG B  94                                                     
SITE     1 BC8  8 ARG A 208  ARG A 211  TYR A 250  HOH A 936                    
SITE     2 BC8  8 HOH A 942  HOH A1018  HOH A1019  HOH A1051                    
SITE     1 BC9 21 ALA A  52  TYR A  53  ALA A  69  LYS A  71                    
SITE     2 BC9 21 ILE A  73  TYR A  81  ARG A  84  THR A  85                    
SITE     3 BC9 21 GLU A  88  GLN A 122  ASP A 123  MET A 125                    
SITE     4 BC9 21 GLU A 126  THR A 127  LYS A 131  LEU A 173                    
SITE     5 BC9 21 ASP A 184  GLY A 186  HOH A 517  HOH A 856                    
SITE     6 BC9 21 HOH A1017                                                     
SITE     1 CC1  6 ARG B 189  ILE B 190  ASP B 192  TYR B 222                    
SITE     2 CC1  6 PHE B 348  HOH B 847                                          
SITE     1 CC2  8 ARG B  84  ARG B  87  GLY B 186  LEU B 187                    
SITE     2 CC2  8 ALA B 188  ARG B 189  HOH B 848  HOH B 981                    
SITE     1 CC3  3 TYR B 130  SER B 170  HOH B 751                               
SITE     1 CC4  5 ASP B  37  ALA B 109  HOH B 738  HOH B 802                    
SITE     2 CC4  5 HOH B 807                                                     
SITE     1 CC5  3 SER B 263  PRO B 285  HOH B 634                               
SITE     1 CC6  2 LEU B 201  GLU B 203                                          
SITE     1 CC7  7 LEU B 133  LYS B 134  GLU B 237  ASN B 241                    
SITE     2 CC7  7 ARG B 242  PRO B 243  HOH B 931                               
SITE     1 CC8  6 LEU B 239  LYS B 298  SER B 299  HOH B 610                    
SITE     2 CC8  6 HOH B 665  HOH B 996                                          
SITE     1 CC9  5 ARG A  94  HIS B 197  ASN B 218  ILE B 273                    
SITE     2 CC9  5 ASN B 274                                                     
SITE     1 DC1  2 HIS B  78  GLN B  79                                          
SITE     1 DC2  7 ARG B 208  ARG B 211  TYR B 250  HOH B 521                    
SITE     2 DC2  7 HOH B 592  HOH B 760  HOH B 960                               
SITE     1 DC3 22 ALA B  52  TYR B  53  ALA B  69  LYS B  71                    
SITE     2 DC3 22 ILE B  73  TYR B  81  ARG B  84  THR B  85                    
SITE     3 DC3 22 GLU B  88  GLN B 122  ASP B 123  MET B 125                    
SITE     4 DC3 22 GLU B 126  THR B 127  LYS B 131  LEU B 173                    
SITE     5 DC3 22 ASP B 184  GLY B 186  HOH B 541  HOH B 578                    
SITE     6 DC3 22 HOH B 971  HOH B 972                                          
CRYST1   61.980   94.010   65.360  90.00  91.71  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016134  0.000000  0.000482        0.00000                         
SCALE2      0.000000  0.010637  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015307        0.00000                         
ATOM      1  N   VAL A  24      38.456  71.796  27.369  1.00 45.99           N  
ANISOU    1  N   VAL A  24     5945   5852   5675   -102     35    235       N  
ATOM      2  CA  VAL A  24      39.876  72.055  26.951  1.00 45.57           C  
ANISOU    2  CA  VAL A  24     5892   5802   5619   -123     47    238       C  
ATOM      3  C   VAL A  24      40.560  70.696  26.773  1.00 45.60           C  
ANISOU    3  C   VAL A  24     5877   5832   5617   -130     48    215       C  
ATOM      4  O   VAL A  24      40.551  69.872  27.697  1.00 43.80           O  
ANISOU    4  O   VAL A  24     5640   5602   5400   -128     44    194       O  
ATOM      5  CB  VAL A  24      40.658  72.933  27.994  1.00 47.27           C  
ANISOU    5  CB  VAL A  24     6117   5987   5856   -137     53    237       C  
ATOM      6  CG1 VAL A  24      42.030  73.358  27.453  1.00 46.48           C  
ANISOU    6  CG1 VAL A  24     6018   5891   5753   -159     65    245       C  
ATOM      7  CG2 VAL A  24      39.857  74.174  28.374  1.00 48.59           C  
ANISOU    7  CG2 VAL A  24     6305   6125   6033   -127     51    255       C  
ATOM      8  N   PRO A  25      41.137  70.441  25.582  1.00 46.28           N  
ANISOU    8  N   PRO A  25     5957   5942   5684   -138     55    221       N  
ATOM      9  CA  PRO A  25      41.739  69.110  25.320  1.00 44.50           C  
ANISOU    9  CA  PRO A  25     5715   5741   5450   -142     58    199       C  
ATOM     10  C   PRO A  25      42.903  68.796  26.258  1.00 38.41           C  
ANISOU   10  C   PRO A  25     4935   4962   4696   -155     63    183       C  
ATOM     11  O   PRO A  25      43.768  69.654  26.460  1.00 36.31           O  
ANISOU   11  O   PRO A  25     4674   4683   4438   -170     71    193       O  
ATOM     12  CB  PRO A  25      42.246  69.209  23.866  1.00 47.12           C  
ANISOU   12  CB  PRO A  25     6046   6098   5759   -149     67    212       C  
ATOM     13  CG  PRO A  25      42.138  70.645  23.463  1.00 48.75           C  
ANISOU   13  CG  PRO A  25     6268   6290   5963   -152     71    241       C  
ATOM     14  CD  PRO A  25      41.501  71.448  24.562  1.00 48.53           C  
ANISOU   14  CD  PRO A  25     6252   6229   5956   -146     64    246       C  
ATOM     15  N   GLY A  26      42.902  67.592  26.849  1.00 34.62           N  
ANISOU   15  N   GLY A  26     4442   4489   4221   -151     59    159       N  
ATOM     16  CA  GLY A  26      43.976  67.159  27.761  1.00 30.63           C  
ANISOU   16  CA  GLY A  26     3928   3980   3732   -161     63    143       C  
ATOM     17  C   GLY A  26      43.881  67.776  29.157  1.00 26.84           C  
ANISOU   17  C   GLY A  26     3454   3470   3274   -163     58    141       C  
ATOM     18  O   GLY A  26      44.818  67.704  29.940  1.00 25.63           O  
ANISOU   18  O   GLY A  26     3295   3311   3133   -174     61    132       O  
ATOM     19  N   GLU A  27      42.749  68.416  29.441  1.00 24.16           N  
ANISOU   19  N   GLU A  27     3128   3114   2938   -151     50    150       N  
ATOM     20  CA  GLU A  27      42.565  69.109  30.691  1.00 24.28           C  
ANISOU   20  CA  GLU A  27     3152   3101   2972   -152     46    150       C  
ATOM     21  C   GLU A  27      42.627  68.096  31.841  1.00 20.43           C  
ANISOU   21  C   GLU A  27     2653   2612   2496   -148     41    126       C  
ATOM     22  O   GLU A  27      42.289  66.923  31.708  1.00 22.32           O  
ANISOU   22  O   GLU A  27     2881   2869   2731   -139     37    113       O  
ATOM     23  CB  GLU A  27      41.214  69.824  30.724  1.00 27.61           C  
ANISOU   23  CB  GLU A  27     3589   3508   3394   -136     40    163       C  
ATOM     24  CG  GLU A  27      40.038  68.847  30.640  1.00 31.66           C  
ANISOU   24  CG  GLU A  27     4094   4035   3901   -117     30    154       C  
ATOM     25  CD  GLU A  27      38.673  69.500  30.739  1.00 36.52           C  
ANISOU   25  CD  GLU A  27     4721   4638   4517   -100     23    167       C  
ATOM     26  OE1 GLU A  27      38.587  70.694  31.120  1.00 40.99           O  
ANISOU   26  OE1 GLU A  27     5303   5180   5093   -101     25    180       O  
ATOM     27  OE2 GLU A  27      37.677  68.787  30.453  1.00 43.04           O  
ANISOU   27  OE2 GLU A  27     5540   5478   5336    -87     15    163       O  
ATOM     28  N   VAL A  28      43.043  68.576  32.985  1.00 16.77           N  
ANISOU   28  N   VAL A  28     2194   2128   2049   -155     40    122       N  
ATOM     29  CA  VAL A  28      42.851  67.812  34.207  1.00 14.69           C  
ANISOU   29  CA  VAL A  28     1924   1860   1798   -149     33    103       C  
ATOM     30  C   VAL A  28      41.469  68.184  34.718  1.00 14.15           C  
ANISOU   30  C   VAL A  28     1867   1776   1734   -132     26    107       C  
ATOM     31  O   VAL A  28      41.207  69.347  35.088  1.00 14.30           O  
ANISOU   31  O   VAL A  28     1902   1772   1759   -132     26    118       O  
ATOM     32  CB  VAL A  28      43.932  68.123  35.242  1.00 14.25           C  
ANISOU   32  CB  VAL A  28     1867   1793   1757   -164     36     96       C  
ATOM     33  CG1 VAL A  28      43.631  67.460  36.572  1.00 14.36           C  
ANISOU   33  CG1 VAL A  28     1875   1799   1781   -156     28     78       C  
ATOM     34  CG2 VAL A  28      45.300  67.716  34.731  1.00 14.48           C  
ANISOU   34  CG2 VAL A  28     1882   1840   1781   -180     44     93       C  
ATOM     35  N   GLU A  29      40.559  67.209  34.752  1.00 13.74           N  
ANISOU   35  N   GLU A  29     1808   1735   1680   -117     19     98       N  
ATOM     36  CA  GLU A  29      39.213  67.453  35.243  1.00 13.52           C  
ANISOU   36  CA  GLU A  29     1787   1695   1656   -100     11    101       C  
ATOM     37  C   GLU A  29      39.156  67.596  36.739  1.00 13.87           C  
ANISOU   37  C   GLU A  29     1836   1720   1716    -98      8     91       C  
ATOM     38  O   GLU A  29      39.872  66.931  37.480  1.00 13.40           O  
ANISOU   38  O   GLU A  29     1767   1662   1663   -104      8     76       O  
ATOM     39  CB  GLU A  29      38.257  66.322  34.803  1.00 13.96           C  
ANISOU   39  CB  GLU A  29     1832   1770   1703    -86      5     95       C  
ATOM     40  CG  GLU A  29      38.132  66.155  33.281  1.00 14.94           C  
ANISOU   40  CG  GLU A  29     1953   1915   1808    -87      6    104       C  
ATOM     41  CD  GLU A  29      36.947  65.303  32.819  1.00 16.08           C  
ANISOU   41  CD  GLU A  29     2089   2076   1944    -73     -2    101       C  
ATOM     42  OE1 GLU A  29      35.955  65.188  33.528  1.00 16.23           O  
ANISOU   42  OE1 GLU A  29     2109   2087   1971    -61     -9     98       O  
ATOM     43  OE2 GLU A  29      37.037  64.783  31.690  1.00 21.01           O  
ANISOU   43  OE2 GLU A  29     2708   2721   2553    -75     -1    101       O  
ATOM     44  N   MET A  30      38.289  68.484  37.180  1.00 12.90           N  
ANISOU   44  N   MET A  30     1727   1578   1598    -87      6    100       N  
ATOM     45  CA  MET A  30      38.162  68.817  38.579  1.00 13.63           C  
ANISOU   45  CA  MET A  30     1826   1649   1703    -85      4     92       C  
ATOM     46  C   MET A  30      36.885  68.241  39.083  1.00 13.74           C  
ANISOU   46  C   MET A  30     1836   1666   1720    -65     -2     88       C  
ATOM     47  O   MET A  30      35.862  68.347  38.410  1.00 15.18           O  
ANISOU   47  O   MET A  30     2019   1853   1895    -52     -5     99       O  
ATOM     48  CB  MET A  30      38.141  70.344  38.800  1.00 14.67           C  
ANISOU   48  CB  MET A  30     1980   1755   1841    -87      8    105       C  
ATOM     49  CG  MET A  30      39.359  71.071  38.275  1.00 15.03           C  
ANISOU   49  CG  MET A  30     2031   1796   1885   -108     16    112       C  
ATOM     50  SD  MET A  30      40.829  70.581  39.225  1.00 15.54           S  
ANISOU   50  SD  MET A  30     2084   1861   1957   -129     16     93       S  
ATOM     51  CE  MET A  30      42.116  70.987  38.031  1.00 17.20           C  
ANISOU   51  CE  MET A  30     2292   2082   2160   -151     25    105       C  
ATOM     52  N   VAL A  31      36.939  67.700  40.281  1.00 12.77           N  
ANISOU   52  N   VAL A  31     1709   1538   1606    -63     -5     72       N  
ATOM     53  CA  VAL A  31      35.754  67.219  41.006  1.00 13.59           C  
ANISOU   53  CA  VAL A  31     1809   1641   1714    -46    -11     68       C  
ATOM     54  C   VAL A  31      35.723  67.908  42.333  1.00 13.77           C  
ANISOU   54  C   VAL A  31     1843   1640   1747    -43    -10     63       C  
ATOM     55  O   VAL A  31      36.596  67.692  43.189  1.00 14.37           O  
ANISOU   55  O   VAL A  31     1917   1712   1828    -54     -9     51       O  
ATOM     56  CB  VAL A  31      35.784  65.699  41.181  1.00 14.44           C  
ANISOU   56  CB  VAL A  31     1898   1767   1821    -45    -15     53       C  
ATOM     57  CG1 VAL A  31      34.473  65.241  41.830  1.00 15.12           C  
ANISOU   57  CG1 VAL A  31     1980   1854   1911    -27    -20     51       C  
ATOM     58  CG2 VAL A  31      35.964  64.996  39.831  1.00 16.02           C  
ANISOU   58  CG2 VAL A  31     2087   1989   2010    -50    -15     55       C  
ATOM     59  N   LYS A  32      34.752  68.811  42.498  1.00 13.74           N  
ANISOU   59  N   LYS A  32     1854   1622   1745    -29     -9     74       N  
ATOM     60  CA  LYS A  32      34.606  69.533  43.711  1.00 15.31           C  
ANISOU   60  CA  LYS A  32     2067   1798   1953    -25     -7     70       C  
ATOM     61  C   LYS A  32      35.968  70.152  44.155  1.00 15.86           C  
ANISOU   61  C   LYS A  32     2146   1854   2027    -46     -4     63       C  
ATOM     62  O   LYS A  32      36.416  70.042  45.307  1.00 16.98           O  
ANISOU   62  O   LYS A  32     2290   1989   2175    -51     -5     50       O  
ATOM     63  CB  LYS A  32      33.949  68.603  44.766  1.00 15.94           C  
ANISOU   63  CB  LYS A  32     2136   1883   2036    -13    -12     57       C  
ATOM     64  CG  LYS A  32      33.095  69.352  45.746  1.00 15.88           C  
ANISOU   64  CG  LYS A  32     2142   1856   2034      2    -10     58       C  
ATOM     65  CD  LYS A  32      32.617  68.500  46.878  1.00 14.59           C  
ANISOU   65  CD  LYS A  32     1970   1699   1876     11    -13     46       C  
ATOM     66  CE  LYS A  32      32.127  69.416  47.996  1.00 15.71           C  
ANISOU   66  CE  LYS A  32     2129   1818   2022     23     -9     45       C  
ATOM     67  NZ  LYS A  32      31.653  68.637  49.158  1.00 14.66           N  
ANISOU   67  NZ  LYS A  32     1988   1691   1893     32    -11     33       N  
ATOM     68  N   GLY A  33      36.618  70.814  43.198  1.00 15.33           N  
ANISOU   68  N   GLY A  33     2085   1784   1956    -58      0     74       N  
ATOM     69  CA  GLY A  33      37.903  71.506  43.459  1.00 16.73           C  
ANISOU   69  CA  GLY A  33     2270   1948   2136    -81      4     71       C  
ATOM     70  C   GLY A  33      39.119  70.601  43.565  1.00 16.14           C  
ANISOU   70  C   GLY A  33     2179   1892   2062    -98      2     58       C  
ATOM     71  O   GLY A  33      40.217  71.070  43.860  1.00 16.81           O  
ANISOU   71  O   GLY A  33     2267   1969   2150   -117      4     54       O  
ATOM     72  N   GLN A  34      38.951  69.294  43.360  1.00 14.62           N  
ANISOU   72  N   GLN A  34     1967   1722   1865    -92     -1     51       N  
ATOM     73  CA AGLN A  34      40.055  68.304  43.465  0.50 15.09           C  
ANISOU   73  CA AGLN A  34     2009   1800   1925   -105     -2     40       C  
ATOM     74  CA BGLN A  34      40.077  68.413  43.432  0.50 14.77           C  
ANISOU   74  CA BGLN A  34     1969   1757   1884   -106     -2     40       C  
ATOM     75  C   GLN A  34      40.400  67.831  42.058  1.00 13.59           C  
ANISOU   75  C   GLN A  34     1808   1630   1727   -110      1     46       C  
ATOM     76  O   GLN A  34      39.549  67.302  41.351  1.00 12.72           O  
ANISOU   76  O   GLN A  34     1692   1531   1609    -97     -1     51       O  
ATOM     77  CB AGLN A  34      39.664  67.050  44.292  0.50 16.52           C  
ANISOU   77  CB AGLN A  34     2176   1991   2109    -94     -8     26       C  
ATOM     78  CB BGLN A  34      39.840  67.378  44.502  0.50 15.96           C  
ANISOU   78  CB BGLN A  34     2109   1915   2040    -98     -7     26       C  
ATOM     79  CG AGLN A  34      38.867  67.266  45.598  0.50 19.14           C  
ANISOU   79  CG AGLN A  34     2516   2308   2447    -82    -11     20       C  
ATOM     80  CG BGLN A  34      39.704  68.064  45.876  0.50 17.46           C  
ANISOU   80  CG BGLN A  34     2314   2084   2238    -96     -9     19       C  
ATOM     81  CD AGLN A  34      39.672  67.937  46.722  0.50 22.21           C  
ANISOU   81  CD AGLN A  34     2916   2682   2842    -94    -11     12       C  
ATOM     82  CD BGLN A  34      39.466  67.080  47.026  0.50 19.65           C  
ANISOU   82  CD BGLN A  34     2581   2368   2519    -88    -14      6       C  
ATOM     83  OE1AGLN A  34      40.771  68.437  46.503  0.50 23.77           O  
ANISOU   83  OE1AGLN A  34     3114   2876   3039   -113     -9     13       O  
ATOM     84  OE1BGLN A  34      38.642  67.330  47.945  0.50 23.37           O  
ANISOU   84  OE1BGLN A  34     3061   2827   2993    -76    -15      3       O  
ATOM     85  NE2AGLN A  34      39.095  67.964  47.947  0.50 24.94           N  
ANISOU   85  NE2AGLN A  34     3268   3017   3192    -84    -14      4       N  
ATOM     86  NE2BGLN A  34      40.160  65.978  46.990  0.50 19.30           N  
ANISOU   86  NE2BGLN A  34     2519   2342   2474    -94    -15     -2       N  
ATOM     87  N   PRO A  35      41.680  67.953  41.643  1.00 12.67           N  
ANISOU   87  N   PRO A  35     1686   1519   1608   -129      5     47       N  
ATOM     88  CA  PRO A  35      42.048  67.424  40.360  1.00 12.33           C  
ANISOU   88  CA  PRO A  35     1632   1498   1556   -132      9     52       C  
ATOM     89  C   PRO A  35      42.004  65.920  40.358  1.00 13.08           C  
ANISOU   89  C   PRO A  35     1708   1613   1648   -125      6     39       C  
ATOM     90  O   PRO A  35      42.514  65.267  41.316  1.00 14.24           O  
ANISOU   90  O   PRO A  35     1846   1762   1802   -127      4     26       O  
ATOM     91  CB  PRO A  35      43.500  67.924  40.145  1.00 12.82           C  
ANISOU   91  CB  PRO A  35     1692   1561   1618   -155     15     54       C  
ATOM     92  CG  PRO A  35      43.883  68.672  41.339  1.00 13.91           C  
ANISOU   92  CG  PRO A  35     1840   1679   1767   -164     13     49       C  
ATOM     93  CD  PRO A  35      42.781  68.654  42.339  1.00 12.88           C  
ANISOU   93  CD  PRO A  35     1718   1535   1642   -148      7     43       C  
ATOM     94  N   PHE A  36      41.372  65.337  39.371  1.00 12.34           N  
ANISOU   94  N   PHE A  36     1610   1534   1545   -116      6     43       N  
ATOM     95  CA  PHE A  36      41.388  63.879  39.163  1.00 13.12           C  
ANISOU   95  CA  PHE A  36     1692   1652   1641   -110      5     30       C  
ATOM     96  C   PHE A  36      42.141  63.650  37.872  1.00 13.17           C  
ANISOU   96  C   PHE A  36     1691   1676   1636   -119     11     34       C  
ATOM     97  O   PHE A  36      41.534  63.624  36.794  1.00 12.76           O  
ANISOU   97  O   PHE A  36     1641   1633   1573   -113     12     42       O  
ATOM     98  CB  PHE A  36      39.958  63.283  39.067  1.00 13.62           C  
ANISOU   98  CB  PHE A  36     1754   1718   1702    -93     -2     29       C  
ATOM     99  CG  PHE A  36      39.384  62.836  40.365  1.00 12.56           C  
ANISOU   99  CG  PHE A  36     1619   1576   1579    -83     -7     20       C  
ATOM    100  CD1 PHE A  36      39.069  63.733  41.339  1.00 12.92           C  
ANISOU  100  CD1 PHE A  36     1677   1602   1632    -81     -9     23       C  
ATOM    101  CD2 PHE A  36      39.029  61.490  40.558  1.00 11.73           C  
ANISOU  101  CD2 PHE A  36     1501   1481   1474    -76    -11      8       C  
ATOM    102  CE1 PHE A  36      38.505  63.319  42.509  1.00 13.00           C  
ANISOU  102  CE1 PHE A  36     1684   1604   1649    -71    -13     15       C  
ATOM    103  CE2 PHE A  36      38.453  61.070  41.726  1.00 12.09           C  
ANISOU  103  CE2 PHE A  36     1545   1519   1529    -67    -15      1       C  
ATOM    104  CZ  PHE A  36      38.185  61.983  42.709  1.00 12.82           C  
ANISOU  104  CZ  PHE A  36     1648   1593   1628    -64    -17      5       C  
ATOM    105  N   ASP A  37      43.471  63.511  37.977  1.00 12.92           N  
ANISOU  105  N   ASP A  37     1650   1650   1607   -132     17     30       N  
ATOM    106  CA  ASP A  37      44.359  63.355  36.825  1.00 13.76           C  
ANISOU  106  CA  ASP A  37     1749   1774   1703   -142     25     33       C  
ATOM    107  C   ASP A  37      44.388  61.922  36.349  1.00 13.66           C  
ANISOU  107  C   ASP A  37     1723   1782   1686   -134     26     21       C  
ATOM    108  O   ASP A  37      45.327  61.151  36.594  1.00 14.07           O  
ANISOU  108  O   ASP A  37     1761   1842   1741   -138     30     11       O  
ATOM    109  CB  ASP A  37      45.746  63.822  37.214  1.00 15.01           C  
ANISOU  109  CB  ASP A  37     1903   1932   1869   -159     31     34       C  
ATOM    110  CG  ASP A  37      46.682  63.915  36.062  1.00 16.42           C  
ANISOU  110  CG  ASP A  37     2075   2126   2037   -170     41     41       C  
ATOM    111  OD1 ASP A  37      46.277  63.812  34.894  1.00 17.55           O  
ANISOU  111  OD1 ASP A  37     2221   2281   2167   -165     44     47       O  
ATOM    112  OD2 ASP A  37      47.877  64.008  36.332  1.00 18.79           O  
ANISOU  112  OD2 ASP A  37     2367   2432   2342   -183     45     39       O  
ATOM    113  N   VAL A  38      43.362  61.570  35.589  1.00 11.76           N  
ANISOU  113  N   VAL A  38     1486   1547   1435   -123     23     22       N  
ATOM    114  CA  VAL A  38      43.179  60.187  35.129  1.00 11.66           C  
ANISOU  114  CA  VAL A  38     1463   1551   1417   -116     23      9       C  
ATOM    115  C   VAL A  38      42.981  60.025  33.644  1.00 11.94           C  
ANISOU  115  C   VAL A  38     1499   1604   1434   -115     27     14       C  
ATOM    116  O   VAL A  38      42.764  58.904  33.170  1.00 12.37           O  
ANISOU  116  O   VAL A  38     1546   1670   1482   -109     27      2       O  
ATOM    117  CB  VAL A  38      41.991  59.503  35.867  1.00 11.72           C  
ANISOU  117  CB  VAL A  38     1471   1552   1432   -102     14      1       C  
ATOM    118  CG1 VAL A  38      42.295  59.342  37.358  1.00 12.17           C  
ANISOU  118  CG1 VAL A  38     1524   1595   1505   -102     11     -7       C  
ATOM    119  CG2 VAL A  38      40.746  60.321  35.657  1.00 11.68           C  
ANISOU  119  CG2 VAL A  38     1478   1538   1422    -96      7     13       C  
ATOM    120  N   GLY A  39      43.134  61.120  32.894  1.00 13.40           N  
ANISOU  120  N   GLY A  39     1692   1789   1611   -122     31     30       N  
ATOM    121  CA  GLY A  39      43.075  61.075  31.465  1.00 13.93           C  
ANISOU  121  CA  GLY A  39     1760   1873   1658   -123     36     36       C  
ATOM    122  C   GLY A  39      44.384  60.598  30.921  1.00 15.30           C  
ANISOU  122  C   GLY A  39     1924   2064   1827   -131     47     30       C  
ATOM    123  O   GLY A  39      45.410  60.672  31.596  1.00 16.48           O  
ANISOU  123  O   GLY A  39     2066   2208   1987   -139     52     27       O  
ATOM    124  N   PRO A  40      44.389  60.174  29.646  1.00 15.58           N  
ANISOU  124  N   PRO A  40     1958   2119   1844   -130     52     29       N  
ATOM    125  CA  PRO A  40      43.273  60.254  28.720  1.00 15.74           C  
ANISOU  125  CA  PRO A  40     1985   2147   1847   -124     46     36       C  
ATOM    126  C   PRO A  40      42.328  59.048  28.768  1.00 14.57           C  
ANISOU  126  C   PRO A  40     1834   2003   1698   -113     38     19       C  
ATOM    127  O   PRO A  40      41.253  59.086  28.160  1.00 15.28           O  
ANISOU  127  O   PRO A  40     1930   2100   1777   -107     30     24       O  
ATOM    128  CB  PRO A  40      43.966  60.312  27.350  1.00 17.02           C  
ANISOU  128  CB  PRO A  40     2147   2330   1990   -130     57     41       C  
ATOM    129  CG  PRO A  40      45.181  59.571  27.531  1.00 17.03           C  
ANISOU  129  CG  PRO A  40     2136   2340   1996   -134     67     28       C  
ATOM    130  CD  PRO A  40      45.652  59.849  28.947  1.00 17.95           C  
ANISOU  130  CD  PRO A  40     2248   2436   2135   -138     65     26       C  
ATOM    131  N   ARG A  41      42.656  58.004  29.539  1.00 13.53           N  
ANISOU  131  N   ARG A  41     1694   1868   1578   -110     38      1       N  
ATOM    132  CA  ARG A  41      41.812  56.831  29.503  1.00 13.63           C  
ANISOU  132  CA  ARG A  41     1703   1885   1589   -101     31    -14       C  
ATOM    133  C   ARG A  41      40.450  57.109  30.115  1.00 12.85           C  
ANISOU  133  C   ARG A  41     1611   1775   1498    -94     18     -9       C  
ATOM    134  O   ARG A  41      39.420  56.600  29.667  1.00 13.62           O  
ANISOU  134  O   ARG A  41     1710   1879   1588    -88     10    -13       O  
ATOM    135  CB  ARG A  41      42.450  55.626  30.206  1.00 13.38           C  
ANISOU  135  CB  ARG A  41     1662   1852   1571    -98     34    -33       C  
ATOM    136  CG  ARG A  41      41.553  54.439  30.188  1.00 13.18           C  
ANISOU  136  CG  ARG A  41     1636   1828   1545    -91     27    -49       C  
ATOM    137  CD  ARG A  41      42.207  53.212  30.658  1.00 13.27           C  
ANISOU  137  CD  ARG A  41     1638   1837   1565    -88     32    -67       C  
ATOM    138  NE  ARG A  41      41.223  52.125  30.754  1.00 13.06           N  
ANISOU  138  NE  ARG A  41     1612   1809   1541    -81     24    -81       N  
ATOM    139  CZ  ARG A  41      41.508  50.875  31.052  1.00 14.51           C  
ANISOU  139  CZ  ARG A  41     1791   1990   1731    -77     28    -98       C  
ATOM    140  NH1 ARG A  41      42.776  50.464  31.214  1.00 16.54           N  
ANISOU  140  NH1 ARG A  41     2042   2250   1994    -77     39   -104       N  
ATOM    141  NH2 ARG A  41      40.526  50.007  31.158  1.00 15.02           N  
ANISOU  141  NH2 ARG A  41     1857   2051   1798    -74     20   -108       N  
ATOM    142  N   TYR A  42      40.447  57.917  31.174  1.00 11.79           N  
ANISOU  142  N   TYR A  42     1480   1622   1379    -94     15     -1       N  
ATOM    143  CA  TYR A  42      39.226  58.111  31.925  1.00 11.04           C  
ANISOU  143  CA  TYR A  42     1388   1514   1293    -86      4      3       C  
ATOM    144  C   TYR A  42      38.860  59.577  31.885  1.00 11.53           C  
ANISOU  144  C   TYR A  42     1461   1567   1354    -86      3     23       C  
ATOM    145  O   TYR A  42      39.695  60.433  32.247  1.00 12.21           O  
ANISOU  145  O   TYR A  42     1551   1643   1446    -93      9     31       O  
ATOM    146  CB  TYR A  42      39.387  57.668  33.362  1.00 10.79           C  
ANISOU  146  CB  TYR A  42     1352   1468   1281    -83      2     -7       C  
ATOM    147  CG  TYR A  42      39.767  56.191  33.544  1.00 10.34           C  
ANISOU  147  CG  TYR A  42     1285   1417   1228    -82      4    -27       C  
ATOM    148  CD1 TYR A  42      38.814  55.203  33.470  1.00 10.46           C  
ANISOU  148  CD1 TYR A  42     1297   1435   1241    -75     -2    -37       C  
ATOM    149  CD2 TYR A  42      41.073  55.799  33.731  1.00 10.31           C  
ANISOU  149  CD2 TYR A  42     1274   1416   1229    -87     13    -35       C  
ATOM    150  CE1 TYR A  42      39.152  53.863  33.647  1.00 10.52           C  
ANISOU  150  CE1 TYR A  42     1297   1446   1254    -74      0    -55       C  
ATOM    151  CE2 TYR A  42      41.422  54.488  33.886  1.00 10.31           C  
ANISOU  151  CE2 TYR A  42     1265   1419   1233    -83     16    -51       C  
ATOM    152  CZ  TYR A  42      40.454  53.485  33.858  1.00 10.04           C  
ANISOU  152  CZ  TYR A  42     1231   1386   1199    -77      9    -62       C  
ATOM    153  OH  TYR A  42      40.805  52.184  34.082  1.00 10.68           O  
ANISOU  153  OH  TYR A  42     1305   1468   1285    -73     12    -78       O  
ATOM    154  N   THR A  43      37.636  59.901  31.461  1.00 12.10           N  
ANISOU  154  N   THR A  43     1538   1642   1418    -78     -5     33       N  
ATOM    155  CA  THR A  43      37.190  61.316  31.363  1.00 12.76           C  
ANISOU  155  CA  THR A  43     1632   1715   1500    -76     -6     54       C  
ATOM    156  C   THR A  43      35.742  61.463  31.812  1.00 12.91           C  
ANISOU  156  C   THR A  43     1654   1728   1523    -63    -17     59       C  
ATOM    157  O   THR A  43      35.095  60.469  32.156  1.00 12.53           O  
ANISOU  157  O   THR A  43     1597   1684   1479    -58    -24     47       O  
ATOM    158  CB  THR A  43      37.298  61.880  29.922  1.00 13.45           C  
ANISOU  158  CB  THR A  43     1725   1818   1567    -80     -3     69       C  
ATOM    159  OG1 THR A  43      36.318  61.223  29.081  1.00 15.14           O  
ANISOU  159  OG1 THR A  43     1936   2051   1767    -73    -11     66       O  
ATOM    160  CG2 THR A  43      38.687  61.731  29.352  1.00 13.31           C  
ANISOU  160  CG2 THR A  43     1705   1810   1543    -92      9     65       C  
ATOM    161  N   GLN A  44      35.178  62.641  31.740  1.00 14.41           N  
ANISOU  161  N   GLN A  44     1854   1909   1713    -58    -19     78       N  
ATOM    162  CA  GLN A  44      33.785  62.884  32.106  1.00 14.96           C  
ANISOU  162  CA  GLN A  44     1924   1973   1786    -44    -28     86       C  
ATOM    163  C   GLN A  44      33.512  62.448  33.542  1.00 14.02           C  
ANISOU  163  C   GLN A  44     1801   1840   1685    -39    -30     74       C  
ATOM    164  O   GLN A  44      32.584  61.703  33.868  1.00 13.85           O  
ANISOU  164  O   GLN A  44     1772   1824   1667    -31    -38     67       O  
ATOM    165  CB  GLN A  44      32.820  62.256  31.075  1.00 17.59           C  
ANISOU  165  CB  GLN A  44     2250   2330   2103    -39    -36     87       C  
ATOM    166  CG  GLN A  44      32.661  63.138  29.876  1.00 21.17           C  
ANISOU  166  CG  GLN A  44     2712   2794   2540    -38    -36    107       C  
ATOM    167  CD  GLN A  44      33.839  63.074  28.962  1.00 25.35           C  
ANISOU  167  CD  GLN A  44     3243   3334   3057    -51    -27    105       C  
ATOM    168  OE1 GLN A  44      34.117  62.013  28.403  1.00 29.50           O  
ANISOU  168  OE1 GLN A  44     3760   3878   3573    -56    -27     90       O  
ATOM    169  NE2 GLN A  44      34.564  64.210  28.784  1.00 28.85           N  
ANISOU  169  NE2 GLN A  44     3696   3767   3499    -56    -18    121       N  
ATOM    170  N   LEU A  45      34.317  63.025  34.420  1.00 13.86           N  
ANISOU  170  N   LEU A  45     1787   1801   1677    -43    -24     73       N  
ATOM    171  CA  LEU A  45      34.274  62.753  35.841  1.00 13.98           C  
ANISOU  171  CA  LEU A  45     1802   1802   1710    -40    -25     62       C  
ATOM    172  C   LEU A  45      33.051  63.403  36.476  1.00 14.89           C  
ANISOU  172  C   LEU A  45     1922   1905   1831    -25    -30     72       C  
ATOM    173  O   LEU A  45      32.735  64.594  36.197  1.00 15.59           O  
ANISOU  173  O   LEU A  45     2022   1985   1917    -20    -29     89       O  
ATOM    174  CB  LEU A  45      35.548  63.292  36.533  1.00 15.06           C  
ANISOU  174  CB  LEU A  45     1943   1923   1855    -51    -18     59       C  
ATOM    175  CG  LEU A  45      36.875  62.525  36.403  1.00 16.13           C  
ANISOU  175  CG  LEU A  45     2071   2069   1991    -64    -12     46       C  
ATOM    176  CD1 LEU A  45      36.926  61.427  37.421  1.00 16.77           C  
ANISOU  176  CD1 LEU A  45     2141   2148   2081    -62    -15     29       C  
ATOM    177  CD2 LEU A  45      37.187  61.953  35.019  1.00 16.08           C  
ANISOU  177  CD2 LEU A  45     2058   2083   1968    -70    -10     45       C  
ATOM    178  N   GLN A  46      32.387  62.669  37.336  1.00 14.01           N  
ANISOU  178  N   GLN A  46     1802   1792   1727    -18    -35     62       N  
ATOM    179  CA  GLN A  46      31.233  63.144  38.080  1.00 15.08           C  
ANISOU  179  CA  GLN A  46     1942   1918   1871     -3    -38     70       C  
ATOM    180  C   GLN A  46      31.364  62.708  39.516  1.00 13.43           C  
ANISOU  180  C   GLN A  46     1731   1698   1676     -2    -38     57       C  
ATOM    181  O   GLN A  46      31.637  61.532  39.802  1.00 14.42           O  
ANISOU  181  O   GLN A  46     1844   1830   1803     -6    -39     42       O  
ATOM    182  CB  GLN A  46      29.900  62.642  37.460  1.00 17.34           C  
ANISOU  182  CB  GLN A  46     2217   2221   2149      7    -47     75       C  
ATOM    183  CG  GLN A  46      29.744  63.059  36.002  1.00 21.17           C  
ANISOU  183  CG  GLN A  46     2705   2721   2618      6    -49     88       C  
ATOM    184  CD  GLN A  46      28.634  62.312  35.284  1.00 25.18           C  
ANISOU  184  CD  GLN A  46     3200   3250   3116     11    -58     89       C  
ATOM    185  OE1 GLN A  46      27.798  61.668  35.914  1.00 27.63           O  
ANISOU  185  OE1 GLN A  46     3502   3563   3434     18    -63     84       O  
ATOM    186  NE2 GLN A  46      28.640  62.379  33.943  1.00 28.11           N  
ANISOU  186  NE2 GLN A  46     3572   3639   3471      7    -60     97       N  
ATOM    187  N   TYR A  47      31.224  63.639  40.435  1.00 12.33           N  
ANISOU  187  N   TYR A  47     1602   1538   1544      5    -35     62       N  
ATOM    188  CA  TYR A  47      31.276  63.323  41.861  1.00 11.65           C  
ANISOU  188  CA  TYR A  47     1515   1441   1470      7    -34     50       C  
ATOM    189  C   TYR A  47      30.249  62.275  42.363  1.00 11.78           C  
ANISOU  189  C   TYR A  47     1518   1467   1490     17    -39     45       C  
ATOM    190  O   TYR A  47      29.074  62.295  41.928  1.00 13.26           O  
ANISOU  190  O   TYR A  47     1701   1663   1674     28    -44     54       O  
ATOM    191  CB  TYR A  47      31.029  64.617  42.646  1.00 11.77           C  
ANISOU  191  CB  TYR A  47     1547   1435   1492     16    -30     58       C  
ATOM    192  CG  TYR A  47      30.951  64.532  44.132  1.00 12.15           C  
ANISOU  192  CG  TYR A  47     1596   1470   1549     21    -29     49       C  
ATOM    193  CD1 TYR A  47      29.753  64.232  44.773  1.00 12.55           C  
ANISOU  193  CD1 TYR A  47     1642   1523   1604     36    -32     50       C  
ATOM    194  CD2 TYR A  47      32.058  64.838  44.919  1.00 12.68           C  
ANISOU  194  CD2 TYR A  47     1672   1525   1622     10    -26     40       C  
ATOM    195  CE1 TYR A  47      29.666  64.248  46.136  1.00 12.50           C  
ANISOU  195  CE1 TYR A  47     1638   1505   1605     41    -30     42       C  
ATOM    196  CE2 TYR A  47      32.016  64.814  46.283  1.00 13.09           C  
ANISOU  196  CE2 TYR A  47     1727   1567   1681     14    -25     31       C  
ATOM    197  CZ  TYR A  47      30.801  64.535  46.909  1.00 12.66           C  
ANISOU  197  CZ  TYR A  47     1668   1513   1629     30    -26     33       C  
ATOM    198  OH  TYR A  47      30.780  64.644  48.269  1.00 15.61           O  
ANISOU  198  OH  TYR A  47     2046   1875   2008     35    -25     25       O  
ATOM    199  N   ILE A  48      30.711  61.353  43.214  1.00 12.11           N  
ANISOU  199  N   ILE A  48     1553   1509   1539     12    -39     30       N  
ATOM    200  CA  ILE A  48      29.814  60.451  43.893  1.00 12.09           C  
ANISOU  200  CA  ILE A  48     1540   1512   1543     21    -43     25       C  
ATOM    201  C   ILE A  48      29.792  60.761  45.370  1.00 11.83           C  
ANISOU  201  C   ILE A  48     1513   1464   1519     27    -40     22       C  
ATOM    202  O   ILE A  48      28.720  60.858  45.993  1.00 13.21           O  
ANISOU  202  O   ILE A  48     1686   1636   1697     40    -41     26       O  
ATOM    203  CB  ILE A  48      30.189  58.974  43.651  1.00 12.15           C  
ANISOU  203  CB  ILE A  48     1534   1533   1550     12    -45     12       C  
ATOM    204  CG1 ILE A  48      29.934  58.603  42.227  1.00 12.82           C  
ANISOU  204  CG1 ILE A  48     1614   1634   1624      8    -49     15       C  
ATOM    205  CG2 ILE A  48      29.413  58.096  44.612  1.00 13.09           C  
ANISOU  205  CG2 ILE A  48     1644   1652   1676     19    -48      7       C  
ATOM    206  CD1 ILE A  48      30.464  57.234  41.830  1.00 12.70           C  
ANISOU  206  CD1 ILE A  48     1589   1630   1608     -2    -50      1       C  
ATOM    207  N   GLY A  49      30.948  60.861  46.044  1.00 11.47           N  
ANISOU  207  N   GLY A  49     1473   1409   1477     18    -37     13       N  
ATOM    208  CA  GLY A  49      30.972  61.099  47.453  1.00 11.33           C  
ANISOU  208  CA  GLY A  49     1461   1379   1466     23    -34      8       C  
ATOM    209  C   GLY A  49      32.368  61.282  47.973  1.00 11.05           C  
ANISOU  209  C   GLY A  49     1430   1336   1433     10    -32      0       C  
ATOM    210  O   GLY A  49      33.317  61.338  47.199  1.00 10.40           O  
ANISOU  210  O   GLY A  49     1347   1257   1346     -2    -31     -1       O  
ATOM    211  N   GLU A  50      32.486  61.502  49.249  1.00 11.92           N  
ANISOU  211  N   GLU A  50     1546   1436   1547     13    -31     -5       N  
ATOM    212  CA  GLU A  50      33.777  61.766  49.836  1.00 12.59           C  
ANISOU  212  CA  GLU A  50     1636   1514   1634      0    -30    -13       C  
ATOM    213  C   GLU A  50      33.781  61.375  51.284  1.00 13.46           C  
ANISOU  213  C   GLU A  50     1745   1621   1748      4    -30    -21       C  
ATOM    214  O   GLU A  50      32.736  61.091  51.909  1.00 16.43           O  
ANISOU  214  O   GLU A  50     2119   1997   2126     18    -30    -20       O  
ATOM    215  CB  GLU A  50      34.144  63.236  49.680  1.00 13.58           C  
ANISOU  215  CB  GLU A  50     1778   1624   1757     -5    -27     -8       C  
ATOM    216  CG  GLU A  50      33.269  64.132  50.493  1.00 14.87           C  
ANISOU  216  CG  GLU A  50     1956   1771   1921      8    -24     -5       C  
ATOM    217  CD  GLU A  50      33.391  65.586  50.077  1.00 15.43           C  
ANISOU  217  CD  GLU A  50     2046   1827   1992      6    -21      3       C  
ATOM    218  OE1 GLU A  50      34.325  66.255  50.529  1.00 18.81           O  
ANISOU  218  OE1 GLU A  50     2485   2243   2421     -6    -20     -2       O  
ATOM    219  OE2 GLU A  50      32.573  66.037  49.241  1.00 16.81           O  
ANISOU  219  OE2 GLU A  50     2223   1999   2163     15    -20     15       O  
ATOM    220  N   GLY A  51      34.971  61.347  51.837  1.00 12.59           N  
ANISOU  220  N   GLY A  51     1636   1510   1639     -7    -31    -29       N  
ATOM    221  CA  GLY A  51      35.165  60.938  53.229  1.00 12.89           C  
ANISOU  221  CA  GLY A  51     1672   1547   1679     -5    -32    -37       C  
ATOM    222  C   GLY A  51      36.634  61.181  53.597  1.00 13.58           C  
ANISOU  222  C   GLY A  51     1760   1633   1766    -21    -34    -44       C  
ATOM    223  O   GLY A  51      37.406  61.783  52.829  1.00 14.04           O  
ANISOU  223  O   GLY A  51     1822   1689   1822    -34    -33    -43       O  
ATOM    224  N   ALA A  52      37.035  60.710  54.767  1.00 14.58           N  
ANISOU  224  N   ALA A  52     1884   1763   1894    -22    -36    -52       N  
ATOM    225  CA  ALA A  52      38.412  60.907  55.216  1.00 16.17           C  
ANISOU  225  CA  ALA A  52     2085   1966   2095    -37    -38    -58       C  
ATOM    226  C   ALA A  52      39.375  60.267  54.186  1.00 14.06           C  
ANISOU  226  C   ALA A  52     1803   1711   1828    -48    -38    -58       C  
ATOM    227  O   ALA A  52      40.453  60.797  53.893  1.00 16.12           O  
ANISOU  227  O   ALA A  52     2065   1972   2088    -62    -39    -59       O  
ATOM    228  CB  ALA A  52      38.598  60.277  56.618  1.00 17.66           C  
ANISOU  228  CB  ALA A  52     2268   2159   2283    -33    -42    -65       C  
ATOM    229  N   TYR A  53      38.963  59.137  53.610  1.00 14.22           N  
ANISOU  229  N   TYR A  53     1811   1742   1851    -40    -38    -56       N  
ATOM    230  CA  TYR A  53      39.744  58.430  52.597  1.00 13.07           C  
ANISOU  230  CA  TYR A  53     1652   1608   1706    -47    -36    -56       C  
ATOM    231  C   TYR A  53      40.156  59.269  51.373  1.00 12.47           C  
ANISOU  231  C   TYR A  53     1581   1530   1625    -57    -33    -51       C  
ATOM    232  O   TYR A  53      41.174  58.948  50.775  1.00 13.29           O  
ANISOU  232  O   TYR A  53     1676   1644   1730    -67    -32    -53       O  
ATOM    233  CB  TYR A  53      38.991  57.193  52.091  1.00 12.88           C  
ANISOU  233  CB  TYR A  53     1617   1591   1683    -37    -35    -56       C  
ATOM    234  CG  TYR A  53      37.741  57.541  51.324  1.00 13.04           C  
ANISOU  234  CG  TYR A  53     1644   1608   1701    -29    -34    -49       C  
ATOM    235  CD1 TYR A  53      37.775  57.792  49.976  1.00 14.51           C  
ANISOU  235  CD1 TYR A  53     1831   1798   1884    -34    -32    -45       C  
ATOM    236  CD2 TYR A  53      36.523  57.603  51.963  1.00 13.45           C  
ANISOU  236  CD2 TYR A  53     1700   1654   1754    -17    -35    -47       C  
ATOM    237  CE1 TYR A  53      36.627  58.163  49.287  1.00 15.02           C  
ANISOU  237  CE1 TYR A  53     1901   1860   1945    -26    -32    -38       C  
ATOM    238  CE2 TYR A  53      35.356  57.941  51.245  1.00 14.19           C  
ANISOU  238  CE2 TYR A  53     1799   1747   1847     -9    -35    -39       C  
ATOM    239  CZ  TYR A  53      35.452  58.254  49.924  1.00 14.67           C  
ANISOU  239  CZ  TYR A  53     1861   1811   1903    -14    -34    -35       C  
ATOM    240  OH  TYR A  53      34.314  58.599  49.163  1.00 18.62           O  
ANISOU  240  OH  TYR A  53     2363   2311   2400     -7    -34    -27       O  
ATOM    241  N   GLY A  54      39.403  60.330  51.017  1.00 11.42           N  
ANISOU  241  N   GLY A  54     1463   1386   1491    -55    -32    -45       N  
ATOM    242  CA  GLY A  54      39.546  61.001  49.740  1.00 11.86           C  
ANISOU  242  CA  GLY A  54     1523   1442   1543    -62    -29    -38       C  
ATOM    243  C   GLY A  54      38.194  61.240  49.109  1.00 11.41           C  
ANISOU  243  C   GLY A  54     1472   1380   1483    -49    -28    -30       C  
ATOM    244  O   GLY A  54      37.253  61.591  49.794  1.00 11.48           O  
ANISOU  244  O   GLY A  54     1489   1380   1493    -39    -29    -28       O  
ATOM    245  N   MET A  55      38.074  61.014  47.799  1.00 10.77           N  
ANISOU  245  N   MET A  55     1386   1308   1397    -50    -26    -25       N  
ATOM    246  CA  MET A  55      36.850  61.333  47.078  1.00 11.12           C  
ANISOU  246  CA  MET A  55     1436   1351   1438    -40    -26    -15       C  
ATOM    247  C   MET A  55      36.623  60.249  46.042  1.00 10.88           C  
ANISOU  247  C   MET A  55     1392   1337   1403    -38    -27    -16       C  
ATOM    248  O   MET A  55      37.588  59.767  45.404  1.00  9.72           O  
ANISOU  248  O   MET A  55     1238   1200   1254    -48    -25    -20       O  
ATOM    249  CB  MET A  55      37.008  62.678  46.418  1.00 12.14           C  
ANISOU  249  CB  MET A  55     1579   1471   1563    -46    -23     -5       C  
ATOM    250  CG  MET A  55      35.781  63.200  45.703  1.00 12.66           C  
ANISOU  250  CG  MET A  55     1651   1534   1625    -34    -24      6       C  
ATOM    251  SD  MET A  55      36.001  64.940  45.191  1.00 15.35           S  
ANISOU  251  SD  MET A  55     2012   1858   1962    -39    -19     20       S  
ATOM    252  CE  MET A  55      35.978  65.740  46.753  1.00 14.85           C  
ANISOU  252  CE  MET A  55     1963   1773   1907    -37    -19     14       C  
ATOM    253  N   VAL A  56      35.351  59.908  45.834  1.00 10.11           N  
ANISOU  253  N   VAL A  56     1293   1243   1305    -26    -30    -13       N  
ATOM    254  CA AVAL A  56      34.980  58.952  44.791  0.50 10.26           C  
ANISOU  254  CA AVAL A  56     1302   1278   1319    -25    -31    -14       C  
ATOM    255  CA BVAL A  56      34.968  58.943  44.780  0.50 10.48           C  
ANISOU  255  CA BVAL A  56     1330   1306   1347    -25    -31    -14       C  
ATOM    256  C   VAL A  56      34.139  59.643  43.721  1.00 10.51           C  
ANISOU  256  C   VAL A  56     1339   1312   1343    -21    -33     -2       C  
ATOM    257  O   VAL A  56      33.240  60.426  44.036  1.00 10.49           O  
ANISOU  257  O   VAL A  56     1344   1301   1341    -11    -34      7       O  
ATOM    258  CB AVAL A  56      34.305  57.671  45.372  0.50  9.98           C  
ANISOU  258  CB AVAL A  56     1255   1247   1289    -18    -35    -21       C  
ATOM    259  CB BVAL A  56      34.189  57.695  45.294  0.50 10.51           C  
ANISOU  259  CB BVAL A  56     1323   1315   1356    -17    -35    -21       C  
ATOM    260  CG1AVAL A  56      33.106  58.008  46.233  0.50  9.84           C  
ANISOU  260  CG1AVAL A  56     1241   1222   1276     -5    -37    -16       C  
ATOM    261  CG1BVAL A  56      34.263  56.555  44.282  0.50 10.40           C  
ANISOU  261  CG1BVAL A  56     1298   1315   1337    -21    -36    -26       C  
ATOM    262  CG2AVAL A  56      33.876  56.708  44.273  0.50  9.85           C  
ANISOU  262  CG2AVAL A  56     1230   1245   1267    -18    -37    -24       C  
ATOM    263  CG2BVAL A  56      34.712  57.208  46.618  0.50 10.68           C  
ANISOU  263  CG2BVAL A  56     1341   1330   1386    -17    -34    -29       C  
ATOM    264  N   SER A  57      34.424  59.301  42.481  1.00 10.58           N  
ANISOU  264  N   SER A  57     1343   1334   1343    -27    -32     -1       N  
ATOM    265  CA ASER A  57      33.738  59.856  41.315  0.60 10.92           C  
ANISOU  265  CA ASER A  57     1390   1383   1376    -24    -34     10       C  
ATOM    266  CA BSER A  57      33.812  59.872  41.269  0.40 10.85           C  
ANISOU  266  CA BSER A  57     1382   1375   1367    -25    -33     10       C  
ATOM    267  C   SER A  57      33.354  58.715  40.398  1.00 11.13           C  
ANISOU  267  C   SER A  57     1406   1427   1395    -25    -37      5       C  
ATOM    268  O   SER A  57      33.825  57.583  40.583  1.00 11.07           O  
ANISOU  268  O   SER A  57     1390   1425   1391    -29    -36     -8       O  
ATOM    269  CB ASER A  57      34.690  60.769  40.593  0.60 11.22           C  
ANISOU  269  CB ASER A  57     1436   1419   1407    -34    -28     17       C  
ATOM    270  CB BSER A  57      34.865  60.658  40.474  0.40 10.99           C  
ANISOU  270  CB BSER A  57     1406   1392   1377    -36    -28     16       C  
ATOM    271  OG ASER A  57      34.951  61.910  41.404  0.60 11.60           O  
ANISOU  271  OG ASER A  57     1497   1449   1462    -34    -26     23       O  
ATOM    272  OG BSER A  57      35.849  59.809  39.870  0.40 11.28           O  
ANISOU  272  OG BSER A  57     1434   1442   1410    -46    -25      7       O  
ATOM    273  N   SER A  58      32.476  58.987  39.435  1.00 10.86           N  
ANISOU  273  N   SER A  58     1373   1403   1352    -20    -41     14       N  
ATOM    274  CA  SER A  58      32.355  58.118  38.253  1.00 11.21           C  
ANISOU  274  CA  SER A  58     1409   1466   1385    -25    -43     10       C  
ATOM    275  C   SER A  58      33.079  58.763  37.089  1.00 11.05           C  
ANISOU  275  C   SER A  58     1394   1451   1351    -32    -39     17       C  
ATOM    276  O   SER A  58      33.339  59.970  37.087  1.00 11.03           O  
ANISOU  276  O   SER A  58     1403   1441   1349    -32    -36     29       O  
ATOM    277  CB  SER A  58      30.887  57.844  37.924  1.00 11.91           C  
ANISOU  277  CB  SER A  58     1493   1564   1469    -16    -52     15       C  
ATOM    278  OG  SER A  58      30.198  59.065  37.694  1.00 13.16           O  
ANISOU  278  OG  SER A  58     1658   1719   1624     -8    -54     32       O  
ATOM    279  N   ALA A  59      33.482  57.940  36.132  1.00 10.99           N  
ANISOU  279  N   ALA A  59     1381   1459   1333    -39    -38      8       N  
ATOM    280  CA  ALA A  59      34.189  58.325  34.938  1.00 11.34           C  
ANISOU  280  CA  ALA A  59     1430   1515   1365    -47    -34     13       C  
ATOM    281  C   ALA A  59      33.827  57.413  33.804  1.00 11.56           C  
ANISOU  281  C   ALA A  59     1451   1562   1378    -49    -37      6       C  
ATOM    282  O   ALA A  59      33.447  56.299  34.010  1.00 12.55           O  
ANISOU  282  O   ALA A  59     1570   1692   1507    -48    -41     -7       O  
ATOM    283  CB  ALA A  59      35.691  58.258  35.149  1.00 11.15           C  
ANISOU  283  CB  ALA A  59     1405   1486   1344    -56    -24      6       C  
ATOM    284  N   TYR A  60      34.037  57.899  32.590  1.00 12.08           N  
ANISOU  284  N   TYR A  60     1521   1640   1427    -53    -35     15       N  
ATOM    285  CA  TYR A  60      33.933  57.080  31.389  1.00 12.05           C  
ANISOU  285  CA  TYR A  60     1514   1657   1406    -57    -37      7       C  
ATOM    286  C   TYR A  60      35.303  56.514  31.046  1.00 12.69           C  
ANISOU  286  C   TYR A  60     1593   1743   1485    -65    -26     -6       C  
ATOM    287  O   TYR A  60      36.281  57.241  30.950  1.00 11.89           O  
ANISOU  287  O   TYR A  60     1496   1639   1382    -70    -18      2       O  
ATOM    288  CB  TYR A  60      33.421  57.909  30.227  1.00 12.84           C  
ANISOU  288  CB  TYR A  60     1619   1770   1488    -55    -40     24       C  
ATOM    289  CG  TYR A  60      33.157  57.086  28.999  1.00 14.39           C  
ANISOU  289  CG  TYR A  60     1812   1990   1665    -59    -44     15       C  
ATOM    290  CD1 TYR A  60      32.017  56.287  28.893  1.00 15.61           C  
ANISOU  290  CD1 TYR A  60     1961   2154   1818    -57    -55      8       C  
ATOM    291  CD2 TYR A  60      34.060  57.091  27.938  1.00 15.26           C  
ANISOU  291  CD2 TYR A  60     1925   2113   1759    -67    -36     14       C  
ATOM    292  CE1 TYR A  60      31.784  55.553  27.762  1.00 15.38           C  
ANISOU  292  CE1 TYR A  60     1929   2145   1769    -62    -59     -1       C  
ATOM    293  CE2 TYR A  60      33.830  56.350  26.791  1.00 16.85           C  
ANISOU  293  CE2 TYR A  60     2125   2336   1941    -70    -39      5       C  
ATOM    294  CZ  TYR A  60      32.698  55.588  26.719  1.00 16.41           C  
ANISOU  294  CZ  TYR A  60     2065   2289   1883    -68    -51     -3       C  
ATOM    295  OH  TYR A  60      32.469  54.842  25.574  1.00 20.26           O  
ANISOU  295  OH  TYR A  60     2550   2797   2349    -73    -55    -14       O  
ATOM    296  N   ASP A  61      35.364  55.211  30.918  1.00 11.98           N  
ANISOU  296  N   ASP A  61     1498   1661   1394    -67    -27    -24       N  
ATOM    297  CA  ASP A  61      36.570  54.475  30.510  1.00 12.48           C  
ANISOU  297  CA  ASP A  61     1559   1731   1454    -73    -17    -38       C  
ATOM    298  C   ASP A  61      36.556  54.294  28.984  1.00 12.96           C  
ANISOU  298  C   ASP A  61     1621   1813   1491    -77    -15    -39       C  
ATOM    299  O   ASP A  61      35.707  53.562  28.441  1.00 12.88           O  
ANISOU  299  O   ASP A  61     1610   1813   1471    -76    -23    -48       O  
ATOM    300  CB  ASP A  61      36.550  53.112  31.224  1.00 12.54           C  
ANISOU  300  CB  ASP A  61     1559   1732   1474    -71    -17    -58       C  
ATOM    301  CG  ASP A  61      37.701  52.220  30.854  1.00 13.53           C  
ANISOU  301  CG  ASP A  61     1681   1863   1596    -74     -7    -73       C  
ATOM    302  OD1 ASP A  61      38.530  52.575  29.967  1.00 13.19           O  
ANISOU  302  OD1 ASP A  61     1640   1831   1540    -79      2    -70       O  
ATOM    303  OD2 ASP A  61      37.838  51.154  31.517  1.00 14.38           O  
ANISOU  303  OD2 ASP A  61     1784   1963   1717    -72     -6    -88       O  
ATOM    304  N   HIS A  62      37.435  55.005  28.298  1.00 14.00           N  
ANISOU  304  N   HIS A  62     1756   1952   1612    -82     -6    -30       N  
ATOM    305  CA  HIS A  62      37.503  54.951  26.838  1.00 15.32           C  
ANISOU  305  CA  HIS A  62     1926   2140   1753    -85     -4    -30       C  
ATOM    306  C   HIS A  62      38.018  53.630  26.296  1.00 15.65           C  
ANISOU  306  C   HIS A  62     1965   2193   1788    -88      2    -52       C  
ATOM    307  O   HIS A  62      37.873  53.368  25.112  1.00 17.34           O  
ANISOU  307  O   HIS A  62     2182   2426   1980    -90      2    -56       O  
ATOM    308  CB  HIS A  62      38.356  56.087  26.307  1.00 15.74           C  
ANISOU  308  CB  HIS A  62     1984   2197   1798    -90      6    -13       C  
ATOM    309  CG  HIS A  62      37.719  57.404  26.488  1.00 17.01           C  
ANISOU  309  CG  HIS A  62     2152   2350   1961    -88      0     10       C  
ATOM    310  ND1 HIS A  62      36.764  57.894  25.608  1.00 18.50           N  
ANISOU  310  ND1 HIS A  62     2345   2551   2133    -85     -8     24       N  
ATOM    311  CD2 HIS A  62      37.844  58.331  27.466  1.00 16.62           C  
ANISOU  311  CD2 HIS A  62     2105   2281   1929    -87      1     22       C  
ATOM    312  CE1 HIS A  62      36.351  59.072  26.032  1.00 19.42           C  
ANISOU  312  CE1 HIS A  62     2467   2655   2257    -81    -11     43       C  
ATOM    313  NE2 HIS A  62      36.993  59.362  27.158  1.00 17.37           N  
ANISOU  313  NE2 HIS A  62     2207   2375   2018    -82     -6     42       N  
ATOM    314  N   VAL A  63      38.641  52.794  27.116  1.00 14.56           N  
ANISOU  314  N   VAL A  63     1821   2044   1666    -86      7    -67       N  
ATOM    315  CA  VAL A  63      39.055  51.482  26.659  1.00 15.51           C  
ANISOU  315  CA  VAL A  63     1939   2172   1781    -86     13    -89       C  
ATOM    316  C   VAL A  63      37.880  50.547  26.717  1.00 15.51           C  
ANISOU  316  C   VAL A  63     1940   2171   1782    -85      1   -102       C  
ATOM    317  O   VAL A  63      37.454  49.956  25.691  1.00 15.72           O  
ANISOU  317  O   VAL A  63     1969   2212   1790    -88     -2   -113       O  
ATOM    318  CB  VAL A  63      40.242  50.954  27.502  1.00 15.88           C  
ANISOU  318  CB  VAL A  63     1979   2207   1845    -85     24    -99       C  
ATOM    319  CG1 VAL A  63      40.520  49.507  27.167  1.00 15.97           C  
ANISOU  319  CG1 VAL A  63     1990   2223   1855    -82     29   -122       C  
ATOM    320  CG2 VAL A  63      41.479  51.826  27.270  1.00 16.27           C  
ANISOU  320  CG2 VAL A  63     2028   2263   1892    -88     37    -87       C  
ATOM    321  N   ARG A  64      37.283  50.390  27.888  1.00 14.91           N  
ANISOU  321  N   ARG A  64     1861   2078   1726    -81     -6   -102       N  
ATOM    322  CA  ARG A  64      36.177  49.451  28.036  1.00 15.31           C  
ANISOU  322  CA  ARG A  64     1911   2127   1781    -81    -17   -114       C  
ATOM    323  C   ARG A  64      34.812  49.983  27.581  1.00 14.25           C  
ANISOU  323  C   ARG A  64     1777   2002   1634    -82    -31   -103       C  
ATOM    324  O   ARG A  64      33.876  49.223  27.468  1.00 14.85           O  
ANISOU  324  O   ARG A  64     1852   2081   1709    -84    -41   -112       O  
ATOM    325  CB  ARG A  64      36.084  48.995  29.484  1.00 16.79           C  
ANISOU  325  CB  ARG A  64     2092   2293   1993    -77    -19   -118       C  
ATOM    326  CG  ARG A  64      37.278  48.157  29.911  1.00 18.23           C  
ANISOU  326  CG  ARG A  64     2272   2468   2186    -75     -7   -132       C  
ATOM    327  CD  ARG A  64      37.237  47.788  31.397  1.00 21.28           C  
ANISOU  327  CD  ARG A  64     2654   2835   2597    -70     -8   -133       C  
ATOM    328  NE  ARG A  64      35.922  47.268  31.770  1.00 23.40           N  
ANISOU  328  NE  ARG A  64     2921   3098   2872    -70    -20   -136       N  
ATOM    329  CZ  ARG A  64      35.270  47.556  32.906  1.00 22.04           C  
ANISOU  329  CZ  ARG A  64     2746   2913   2715    -66    -27   -127       C  
ATOM    330  NH1 ARG A  64      35.808  48.340  33.845  1.00 21.23           N  
ANISOU  330  NH1 ARG A  64     2642   2801   2624    -62    -23   -116       N  
ATOM    331  NH2 ARG A  64      34.088  47.006  33.105  1.00 27.82           N  
ANISOU  331  NH2 ARG A  64     3477   3644   3451    -67    -37   -131       N  
ATOM    332  N   LYS A  65      34.706  51.289  27.336  1.00 15.10           N  
ANISOU  332  N   LYS A  65     1887   2114   1735    -81    -33    -81       N  
ATOM    333  CA  LYS A  65      33.504  51.955  26.837  1.00 15.32           C  
ANISOU  333  CA  LYS A  65     1916   2153   1752    -80    -45    -67       C  
ATOM    334  C   LYS A  65      32.363  51.808  27.812  1.00 15.36           C  
ANISOU  334  C   LYS A  65     1916   2147   1773    -75    -56    -64       C  
ATOM    335  O   LYS A  65      31.258  51.371  27.462  1.00 16.01           O  
ANISOU  335  O   LYS A  65     1995   2239   1848    -77    -68    -68       O  
ATOM    336  CB  LYS A  65      33.097  51.405  25.447  1.00 17.30           C  
ANISOU  336  CB  LYS A  65     2169   2426   1977    -85    -50    -76       C  
ATOM    337  CG  LYS A  65      34.189  51.425  24.419  1.00 19.66           C  
ANISOU  337  CG  LYS A  65     2473   2738   2258    -89    -38    -80       C  
ATOM    338  CD  LYS A  65      34.752  52.758  24.175  1.00 21.17           C  
ANISOU  338  CD  LYS A  65     2669   2932   2444    -88    -31    -58       C  
ATOM    339  CE  LYS A  65      35.575  52.693  22.897  1.00 22.51           C  
ANISOU  339  CE  LYS A  65     2842   3121   2589    -93    -22    -62       C  
ATOM    340  NZ  LYS A  65      36.397  53.922  22.764  1.00 24.28           N  
ANISOU  340  NZ  LYS A  65     3070   3344   2811    -93    -12    -41       N  
ATOM    341  N   THR A  66      32.639  52.133  29.059  1.00 14.13           N  
ANISOU  341  N   THR A  66     1759   1972   1638    -71    -53    -60       N  
ATOM    342  CA  THR A  66      31.652  52.034  30.104  1.00 14.61           C  
ANISOU  342  CA  THR A  66     1815   2022   1716    -65    -61    -57       C  
ATOM    343  C   THR A  66      32.038  52.999  31.211  1.00 13.26           C  
ANISOU  343  C   THR A  66     1645   1832   1560    -59    -56    -44       C  
ATOM    344  O   THR A  66      33.191  53.393  31.322  1.00 13.07           O  
ANISOU  344  O   THR A  66     1625   1803   1539    -61    -46    -43       O  
ATOM    345  CB  THR A  66      31.515  50.594  30.663  1.00 16.46           C  
ANISOU  345  CB  THR A  66     2044   2249   1962    -68    -62    -77       C  
ATOM    346  OG1 THR A  66      30.309  50.495  31.433  1.00 19.47           O  
ANISOU  346  OG1 THR A  66     2419   2625   2354    -64    -72    -72       O  
ATOM    347  CG2 THR A  66      32.678  50.245  31.494  1.00 16.78           C  
ANISOU  347  CG2 THR A  66     2084   2274   2017    -67    -51    -85       C  
ATOM    348  N   ARG A  67      31.094  53.356  32.043  1.00 12.46           N  
ANISOU  348  N   ARG A  67     1541   1722   1470    -53    -63    -35       N  
ATOM    349  CA  ARG A  67      31.382  54.176  33.210  1.00 11.57           C  
ANISOU  349  CA  ARG A  67     1431   1592   1373    -47    -59    -25       C  
ATOM    350  C   ARG A  67      31.786  53.286  34.380  1.00 10.94           C  
ANISOU  350  C   ARG A  67     1347   1498   1311    -47    -55    -39       C  
ATOM    351  O   ARG A  67      31.290  52.161  34.553  1.00 11.12           O  
ANISOU  351  O   ARG A  67     1365   1523   1339    -48    -59    -51       O  
ATOM    352  CB  ARG A  67      30.218  55.088  33.572  1.00 12.09           C  
ANISOU  352  CB  ARG A  67     1498   1655   1442    -37    -66     -8       C  
ATOM    353  CG  ARG A  67      30.005  56.206  32.532  1.00 13.02           C  
ANISOU  353  CG  ARG A  67     1621   1783   1543    -35    -68     10       C  
ATOM    354  CD  ARG A  67      29.025  57.301  32.975  1.00 13.66           C  
ANISOU  354  CD  ARG A  67     1704   1857   1628    -24    -72     29       C  
ATOM    355  NE  ARG A  67      29.543  58.151  34.067  1.00 13.01           N  
ANISOU  355  NE  ARG A  67     1629   1753   1561    -19    -65     35       N  
ATOM    356  CZ  ARG A  67      30.408  59.171  33.946  1.00 12.38           C  
ANISOU  356  CZ  ARG A  67     1560   1664   1480    -21    -57     45       C  
ATOM    357  NH1 ARG A  67      30.887  59.511  32.775  1.00 13.25           N  
ANISOU  357  NH1 ARG A  67     1674   1786   1575    -27    -55     51       N  
ATOM    358  NH2 ARG A  67      30.748  59.854  35.022  1.00 12.48           N  
ANISOU  358  NH2 ARG A  67     1579   1657   1506    -18    -52     48       N  
ATOM    359  N   VAL A  68      32.712  53.810  35.158  1.00 10.04           N  
ANISOU  359  N   VAL A  68     1237   1371   1207    -46    -48    -36       N  
ATOM    360  CA  VAL A  68      33.353  53.130  36.278  1.00 10.22           C  
ANISOU  360  CA  VAL A  68     1256   1382   1246    -46    -43    -47       C  
ATOM    361  C   VAL A  68      33.396  54.087  37.470  1.00  9.78           C  
ANISOU  361  C   VAL A  68     1204   1310   1202    -40    -42    -37       C  
ATOM    362  O   VAL A  68      33.145  55.289  37.299  1.00 10.12           O  
ANISOU  362  O   VAL A  68     1254   1352   1241    -38    -43    -23       O  
ATOM    363  CB  VAL A  68      34.792  52.695  35.913  1.00 10.72           C  
ANISOU  363  CB  VAL A  68     1319   1448   1307    -52    -34    -57       C  
ATOM    364  CG1 VAL A  68      34.758  51.613  34.828  1.00 10.92           C  
ANISOU  364  CG1 VAL A  68     1341   1486   1320    -56    -34    -71       C  
ATOM    365  CG2 VAL A  68      35.653  53.905  35.522  1.00 10.71           C  
ANISOU  365  CG2 VAL A  68     1324   1447   1299    -56    -27    -46       C  
ATOM    366  N   ALA A  69      33.722  53.565  38.649  1.00  9.47           N  
ANISOU  366  N   ALA A  69     1162   1261   1177    -38    -40    -44       N  
ATOM    367  CA  ALA A  69      34.020  54.399  39.802  1.00  9.43           C  
ANISOU  367  CA  ALA A  69     1161   1241   1182    -35    -38    -38       C  
ATOM    368  C   ALA A  69      35.524  54.576  39.889  1.00  9.61           C  
ANISOU  368  C   ALA A  69     1184   1261   1206    -42    -30    -41       C  
ATOM    369  O   ALA A  69      36.281  53.647  39.646  1.00  9.54           O  
ANISOU  369  O   ALA A  69     1169   1257   1197    -46    -26    -52       O  
ATOM    370  CB  ALA A  69      33.493  53.775  41.096  1.00  9.18           C  
ANISOU  370  CB  ALA A  69     1124   1200   1164    -29    -41    -42       C  
ATOM    371  N   ILE A  70      35.949  55.790  40.219  1.00  8.93           N  
ANISOU  371  N   ILE A  70     1105   1167   1121    -44    -28    -32       N  
ATOM    372  CA  ILE A  70      37.379  56.064  40.497  1.00  9.40           C  
ANISOU  372  CA  ILE A  70     1165   1224   1184    -52    -22    -34       C  
ATOM    373  C   ILE A  70      37.470  56.873  41.766  1.00  9.77           C  
ANISOU  373  C   ILE A  70     1217   1255   1239    -50    -22    -30       C  
ATOM    374  O   ILE A  70      36.873  57.916  41.900  1.00  9.63           O  
ANISOU  374  O   ILE A  70     1209   1229   1221    -47    -24    -20       O  
ATOM    375  CB  ILE A  70      38.015  56.857  39.368  1.00  9.91           C  
ANISOU  375  CB  ILE A  70     1234   1295   1237    -60    -17    -27       C  
ATOM    376  CG1 ILE A  70      37.786  56.186  38.012  1.00 10.58           C  
ANISOU  376  CG1 ILE A  70     1315   1395   1308    -61    -16    -30       C  
ATOM    377  CG2 ILE A  70      39.505  57.079  39.681  1.00  9.81           C  
ANISOU  377  CG2 ILE A  70     1219   1281   1228    -69    -10    -29       C  
ATOM    378  CD1 ILE A  70      38.545  56.858  36.871  1.00 10.95           C  
ANISOU  378  CD1 ILE A  70     1366   1452   1343    -69    -10    -23       C  
ATOM    379  N   LYS A  71      38.257  56.364  42.732  1.00  8.54           N  
ANISOU  379  N   LYS A  71     1056   1096   1092    -52    -21    -38       N  
ATOM    380  CA  LYS A  71      38.494  57.085  43.926  1.00  8.57           C  
ANISOU  380  CA  LYS A  71     1065   1087   1104    -53    -22    -36       C  
ATOM    381  C   LYS A  71      39.931  57.574  43.998  1.00  8.59           C  
ANISOU  381  C   LYS A  71     1067   1090   1106    -65    -17    -37       C  
ATOM    382  O   LYS A  71      40.873  56.823  43.618  1.00  8.87           O  
ANISOU  382  O   LYS A  71     1092   1136   1142    -69    -13    -43       O  
ATOM    383  CB  LYS A  71      38.134  56.240  45.183  1.00  8.48           C  
ANISOU  383  CB  LYS A  71     1048   1071   1102    -45    -25    -43       C  
ATOM    384  CG  LYS A  71      38.893  54.927  45.347  1.00  8.42           C  
ANISOU  384  CG  LYS A  71     1029   1072   1099    -46    -23    -54       C  
ATOM    385  CD  LYS A  71      38.260  54.082  46.445  1.00  8.29           C  
ANISOU  385  CD  LYS A  71     1008   1051   1090    -37    -27    -58       C  
ATOM    386  CE  LYS A  71      38.994  52.776  46.648  1.00  8.23           C  
ANISOU  386  CE  LYS A  71      989   1049   1088    -36    -24    -67       C  
ATOM    387  NZ  LYS A  71      38.223  51.869  47.552  1.00  8.53           N  
ANISOU  387  NZ  LYS A  71     1024   1083   1135    -27    -27    -69       N  
ATOM    388  N   LYS A  72      40.104  58.808  44.500  1.00  8.51           N  
ANISOU  388  N   LYS A  72     1067   1068   1098    -69    -18    -30       N  
ATOM    389  CA  LYS A  72      41.409  59.445  44.619  1.00  8.87           C  
ANISOU  389  CA  LYS A  72     1113   1113   1144    -83    -14    -30       C  
ATOM    390  C   LYS A  72      41.800  59.375  46.077  1.00  9.20           C  
ANISOU  390  C   LYS A  72     1153   1148   1194    -84    -18    -36       C  
ATOM    391  O   LYS A  72      41.147  60.000  46.939  1.00  9.84           O  
ANISOU  391  O   LYS A  72     1245   1216   1279    -79    -21    -35       O  
ATOM    392  CB  LYS A  72      41.361  60.909  44.132  1.00  8.78           C  
ANISOU  392  CB  LYS A  72     1116   1092   1129    -90    -12    -18       C  
ATOM    393  CG  LYS A  72      42.712  61.580  44.260  1.00  9.18           C  
ANISOU  393  CG  LYS A  72     1166   1141   1180   -107     -9    -17       C  
ATOM    394  CD  LYS A  72      42.630  63.056  43.986  1.00  9.44           C  
ANISOU  394  CD  LYS A  72     1215   1160   1211   -114     -7     -6       C  
ATOM    395  CE  LYS A  72      44.010  63.679  43.894  1.00  9.90           C  
ANISOU  395  CE  LYS A  72     1272   1219   1270   -134     -3     -5       C  
ATOM    396  NZ  LYS A  72      43.863  65.126  43.672  1.00 10.69           N  
ANISOU  396  NZ  LYS A  72     1390   1302   1369   -141     -1      6       N  
ATOM    397  N   ILE A  73      42.900  58.726  46.356  1.00  9.39           N  
ANISOU  397  N   ILE A  73     1164   1181   1221    -90    -16    -42       N  
ATOM    398  CA  ILE A  73      43.417  58.599  47.697  1.00  9.72           C  
ANISOU  398  CA  ILE A  73     1203   1220   1269    -91    -20    -48       C  
ATOM    399  C   ILE A  73      44.799  59.270  47.742  1.00  9.88           C  
ANISOU  399  C   ILE A  73     1220   1243   1289   -108    -18    -47       C  
ATOM    400  O   ILE A  73      45.628  59.050  46.853  1.00  9.38           O  
ANISOU  400  O   ILE A  73     1148   1192   1224   -115    -13    -46       O  
ATOM    401  CB  ILE A  73      43.627  57.104  48.081  1.00  9.83           C  
ANISOU  401  CB  ILE A  73     1202   1245   1288    -83    -20    -56       C  
ATOM    402  CG1 ILE A  73      42.467  56.184  47.679  1.00 10.43           C  
ANISOU  402  CG1 ILE A  73     1277   1321   1364    -69    -21    -57       C  
ATOM    403  CG2 ILE A  73      43.970  56.965  49.536  1.00 10.47           C  
ANISOU  403  CG2 ILE A  73     1281   1323   1375    -82    -25    -60       C  
ATOM    404  CD1 ILE A  73      41.166  56.520  48.305  1.00 10.39           C  
ANISOU  404  CD1 ILE A  73     1282   1305   1360    -60    -25    -55       C  
ATOM    405  N   SER A  74      45.013  60.115  48.743  1.00 10.14           N  
ANISOU  405  N   SER A  74     1262   1266   1325   -115    -22    -48       N  
ATOM    406  CA  SER A  74      46.237  60.913  48.857  1.00 11.09           C  
ANISOU  406  CA  SER A  74     1381   1387   1445   -134    -22    -47       C  
ATOM    407  C   SER A  74      46.765  60.802  50.289  1.00 10.64           C  
ANISOU  407  C   SER A  74     1320   1330   1392   -137    -28    -54       C  
ATOM    408  O   SER A  74      46.592  61.695  51.109  1.00 12.47           O  
ANISOU  408  O   SER A  74     1565   1549   1624   -142    -32    -55       O  
ATOM    409  CB  SER A  74      45.932  62.354  48.484  1.00 12.01           C  
ANISOU  409  CB  SER A  74     1515   1487   1559   -142    -20    -39       C  
ATOM    410  OG  SER A  74      45.340  62.426  47.190  1.00 12.54           O  
ANISOU  410  OG  SER A  74     1586   1556   1621   -137    -15    -32       O  
ATOM    411  N   PRO A  75      47.407  59.652  50.628  1.00 10.07           N  
ANISOU  411  N   PRO A  75     1230   1274   1323   -133    -29    -58       N  
ATOM    412  CA  PRO A  75      47.656  59.297  52.005  1.00 10.01           C  
ANISOU  412  CA  PRO A  75     1218   1268   1318   -131    -36    -64       C  
ATOM    413  C   PRO A  75      49.064  59.555  52.518  1.00 10.93           C  
ANISOU  413  C   PRO A  75     1323   1395   1435   -147    -39    -66       C  
ATOM    414  O   PRO A  75      49.398  59.186  53.636  1.00 10.41           O  
ANISOU  414  O   PRO A  75     1251   1335   1371   -145    -46    -70       O  
ATOM    415  CB  PRO A  75      47.432  57.779  51.960  1.00  9.66           C  
ANISOU  415  CB  PRO A  75     1159   1234   1276   -114    -34    -66       C  
ATOM    416  CG  PRO A  75      48.061  57.404  50.663  1.00  9.81           C  
ANISOU  416  CG  PRO A  75     1167   1265   1294   -118    -27    -64       C  
ATOM    417  CD  PRO A  75      47.670  58.510  49.717  1.00 10.06           C  
ANISOU  417  CD  PRO A  75     1213   1288   1322   -126    -24    -58       C  
ATOM    418  N   PHE A  76      49.948  60.091  51.683  1.00 11.36           N  
ANISOU  418  N   PHE A  76     1373   1456   1489   -162    -35    -62       N  
ATOM    419  CA  PHE A  76      51.391  59.968  51.907  1.00 13.10           C  
ANISOU  419  CA  PHE A  76     1575   1692   1710   -176    -37    -62       C  
ATOM    420  C   PHE A  76      52.000  60.862  53.003  1.00 15.46           C  
ANISOU  420  C   PHE A  76     1877   1987   2008   -193    -45    -65       C  
ATOM    421  O   PHE A  76      53.129  60.569  53.464  1.00 16.95           O  
ANISOU  421  O   PHE A  76     2049   2194   2199   -201    -49    -66       O  
ATOM    422  CB  PHE A  76      52.128  60.068  50.558  1.00 12.79           C  
ANISOU  422  CB  PHE A  76     1526   1664   1670   -185    -28    -56       C  
ATOM    423  CG  PHE A  76      51.738  58.977  49.615  1.00 11.96           C  
ANISOU  423  CG  PHE A  76     1413   1566   1564   -168    -20    -55       C  
ATOM    424  CD1 PHE A  76      51.920  57.647  49.952  1.00 11.55           C  
ANISOU  424  CD1 PHE A  76     1346   1526   1515   -153    -20    -59       C  
ATOM    425  CD2 PHE A  76      51.156  59.264  48.407  1.00 12.25           C  
ANISOU  425  CD2 PHE A  76     1459   1597   1597   -166    -13    -51       C  
ATOM    426  CE1 PHE A  76      51.495  56.625  49.100  1.00 11.76           C  
ANISOU  426  CE1 PHE A  76     1369   1558   1543   -138    -14    -60       C  
ATOM    427  CE2 PHE A  76      50.778  58.236  47.555  1.00 11.28           C  
ANISOU  427  CE2 PHE A  76     1330   1482   1472   -152     -7    -52       C  
ATOM    428  CZ  PHE A  76      50.954  56.926  47.932  1.00 11.03           C  
ANISOU  428  CZ  PHE A  76     1285   1460   1445   -138     -7    -57       C  
ATOM    429  N   GLU A  77      51.189  61.762  53.537  1.00 15.30           N  
ANISOU  429  N   GLU A  77     1880   1948   1987   -194    -49    -68       N  
ATOM    430  CA  GLU A  77      51.617  62.611  54.656  1.00 17.37           C  
ANISOU  430  CA  GLU A  77     2149   2204   2247   -210    -58    -73       C  
ATOM    431  C   GLU A  77      51.592  61.922  55.996  1.00 16.54           C  
ANISOU  431  C   GLU A  77     2039   2106   2141   -200    -66    -80       C  
ATOM    432  O   GLU A  77      52.293  62.391  56.925  1.00 16.00           O  
ANISOU  432  O   GLU A  77     1968   2040   2069   -215    -74    -85       O  
ATOM    433  CB  GLU A  77      50.809  63.879  54.697  1.00 20.46           C  
ANISOU  433  CB  GLU A  77     2567   2569   2636   -215    -57    -74       C  
ATOM    434  CG  GLU A  77      51.003  64.673  53.449  1.00 25.65           C  
ANISOU  434  CG  GLU A  77     3231   3220   3294   -227    -50    -66       C  
ATOM    435  CD  GLU A  77      50.344  66.038  53.469  1.00 33.28           C  
ANISOU  435  CD  GLU A  77     4224   4160   4260   -233    -49    -66       C  
ATOM    436  OE1 GLU A  77      49.127  66.161  53.797  1.00 36.83           O  
ANISOU  436  OE1 GLU A  77     4691   4595   4709   -217    -48    -67       O  
ATOM    437  OE2 GLU A  77      51.065  67.011  53.115  1.00 39.30           O  
ANISOU  437  OE2 GLU A  77     4992   4917   5023   -255    -47    -62       O  
ATOM    438  N   HIS A  78      50.844  60.826  56.157  1.00 15.91           N  
ANISOU  438  N   HIS A  78     1955   2030   2062   -178    -65    -80       N  
ATOM    439  CA AHIS A  78      50.750  60.173  57.438  0.50 15.86           C  
ANISOU  439  CA AHIS A  78     1943   2028   2053   -168    -72    -85       C  
ATOM    440  CA BHIS A  78      50.800  60.148  57.454  0.50 15.92           C  
ANISOU  440  CA BHIS A  78     1950   2037   2061   -169    -72    -85       C  
ATOM    441  C   HIS A  78      50.834  58.656  57.363  1.00 14.94           C  
ANISOU  441  C   HIS A  78     1807   1927   1940   -151    -70    -82       C  
ATOM    442  O   HIS A  78      50.192  58.016  56.504  1.00 13.78           O  
ANISOU  442  O   HIS A  78     1659   1778   1797   -138    -62    -79       O  
ATOM    443  CB AHIS A  78      49.485  60.663  58.127  0.50 16.80           C  
ANISOU  443  CB AHIS A  78     2086   2129   2170   -159    -73    -89       C  
ATOM    444  CB BHIS A  78      49.620  60.588  58.339  0.50 16.94           C  
ANISOU  444  CB BHIS A  78     2101   2149   2187   -160    -75    -90       C  
ATOM    445  CG AHIS A  78      49.547  62.120  58.488  0.50 18.30           C  
ANISOU  445  CG AHIS A  78     2294   2303   2355   -176    -77    -93       C  
ATOM    446  CG BHIS A  78      49.836  60.292  59.807  0.50 18.49           C  
ANISOU  446  CG BHIS A  78     2295   2353   2378   -157    -84    -95       C  
ATOM    447  ND1AHIS A  78      48.991  63.115  57.703  0.50 20.14           N  
ANISOU  447  ND1AHIS A  78     2546   2518   2590   -180    -71    -91       N  
ATOM    448  ND1BHIS A  78      49.552  59.064  60.364  0.50 18.85           N  
ANISOU  448  ND1BHIS A  78     2330   2409   2425   -139    -85    -93       N  
ATOM    449  CD2AHIS A  78      50.173  62.751  59.504  0.50 19.55           C  
ANISOU  449  CD2AHIS A  78     2457   2462   2509   -191    -85   -100       C  
ATOM    450  CD2BHIS A  78      50.343  61.049  60.817  0.50 19.51           C  
ANISOU  450  CD2BHIS A  78     2430   2481   2501   -172    -92   -102       C  
ATOM    451  CE1AHIS A  78      49.238  64.290  58.249  0.50 19.80           C  
ANISOU  451  CE1AHIS A  78     2518   2462   2543   -197    -75    -96       C  
ATOM    452  CE1BHIS A  78      49.876  59.060  61.639  0.50 20.20           C  
ANISOU  452  CE1BHIS A  78     2500   2586   2590   -142    -94    -98       C  
ATOM    453  NE2AHIS A  78      49.964  64.098  59.333  0.50 19.78           N  
ANISOU  453  NE2AHIS A  78     2508   2471   2537   -204    -84   -103       N  
ATOM    454  NE2BHIS A  78      50.339  60.266  61.952  0.50 20.62           N  
ANISOU  454  NE2BHIS A  78     2563   2633   2638   -161    -99   -104       N  
ATOM    455  N   GLN A  79      51.572  58.061  58.295  1.00 14.31           N  
ANISOU  455  N   GLN A  79     1713   1863   1860   -150    -76    -83       N  
ATOM    456  CA  GLN A  79      51.754  56.664  58.345  1.00 14.50           C  
ANISOU  456  CA  GLN A  79     1720   1901   1888   -134    -75    -80       C  
ATOM    457  C   GLN A  79      50.430  55.919  58.459  1.00 13.37           C  
ANISOU  457  C   GLN A  79     1585   1747   1747   -113    -71    -80       C  
ATOM    458  O   GLN A  79      50.242  54.868  57.825  1.00 11.77           O  
ANISOU  458  O   GLN A  79     1374   1549   1550   -100    -65    -77       O  
ATOM    459  CB  GLN A  79      52.709  56.313  59.455  1.00 17.03           C  
ANISOU  459  CB  GLN A  79     2025   2239   2206   -137    -84    -80       C  
ATOM    460  CG  GLN A  79      53.256  54.925  59.407  1.00 19.17           C  
ANISOU  460  CG  GLN A  79     2274   2527   2483   -123    -81    -75       C  
ATOM    461  CD  GLN A  79      52.755  54.145  60.504  1.00 24.99           C  
ANISOU  461  CD  GLN A  79     3012   3265   3219   -107    -86    -75       C  
ATOM    462  OE1 GLN A  79      51.563  54.164  60.753  1.00 28.56           O  
ANISOU  462  OE1 GLN A  79     3480   3701   3669    -98    -85    -77       O  
ATOM    463  NE2 GLN A  79      53.681  53.578  61.331  1.00 31.22           N  
ANISOU  463  NE2 GLN A  79     3783   4072   4007   -105    -93    -71       N  
ATOM    464  N   THR A  80      49.490  56.403  59.274  1.00 12.93           N  
ANISOU  464  N   THR A  80     1547   1678   1687   -109    -75    -83       N  
ATOM    465  CA ATHR A  80      48.250  55.686  59.419  0.50 13.14           C  
ANISOU  465  CA ATHR A  80     1581   1697   1716    -90    -71    -82       C  
ATOM    466  CA BTHR A  80      48.229  55.741  59.436  0.50 13.30           C  
ANISOU  466  CA BTHR A  80     1602   1717   1736    -91    -71    -82       C  
ATOM    467  C   THR A  80      47.462  55.658  58.108  1.00 12.39           C  
ANISOU  467  C   THR A  80     1491   1592   1624    -85    -63    -80       C  
ATOM    468  O   THR A  80      46.854  54.609  57.778  1.00 12.42           O  
ANISOU  468  O   THR A  80     1490   1597   1633    -71    -58    -78       O  
ATOM    469  CB ATHR A  80      47.370  56.190  60.565  0.50 13.71           C  
ANISOU  469  CB ATHR A  80     1669   1758   1782    -86    -76    -85       C  
ATOM    470  CB BTHR A  80      47.359  56.430  60.490  0.50 14.14           C  
ANISOU  470  CB BTHR A  80     1726   1811   1836    -88    -76    -86       C  
ATOM    471  OG1ATHR A  80      47.116  57.591  60.411  0.50 14.42           O  
ANISOU  471  OG1ATHR A  80     1777   1835   1868    -98    -76    -89       O  
ATOM    472  OG1BTHR A  80      48.032  56.400  61.763  0.50 15.61           O  
ANISOU  472  OG1BTHR A  80     1907   2007   2016    -92    -84    -88       O  
ATOM    473  CG2ATHR A  80      48.025  55.879  61.940  0.50 14.05           C  
ANISOU  473  CG2ATHR A  80     1705   1814   1821    -86    -84    -87       C  
ATOM    474  CG2BTHR A  80      46.003  55.716  60.589  0.50 14.42           C  
ANISOU  474  CG2BTHR A  80     1767   1838   1874    -69    -71    -83       C  
ATOM    475  N   TYR A  81      47.479  56.750  57.336  1.00 11.06           N  
ANISOU  475  N   TYR A  81     1332   1415   1454    -97    -60    -80       N  
ATOM    476  CA  TYR A  81      46.735  56.762  56.107  1.00 10.65           C  
ANISOU  476  CA  TYR A  81     1287   1357   1405    -93    -53    -77       C  
ATOM    477  C   TYR A  81      47.348  55.791  55.125  1.00  9.77           C  
ANISOU  477  C   TYR A  81     1158   1258   1297    -90    -48    -75       C  
ATOM    478  O   TYR A  81      46.660  55.156  54.343  1.00  8.77           O  
ANISOU  478  O   TYR A  81     1031   1129   1172    -80    -43    -74       O  
ATOM    479  CB  TYR A  81      46.743  58.150  55.501  1.00 11.65           C  
ANISOU  479  CB  TYR A  81     1426   1472   1527   -107    -52    -76       C  
ATOM    480  CG  TYR A  81      46.331  59.317  56.413  1.00 14.47           C  
ANISOU  480  CG  TYR A  81     1802   1815   1880   -112    -56    -79       C  
ATOM    481  CD1 TYR A  81      45.597  59.138  57.541  1.00 15.52           C  
ANISOU  481  CD1 TYR A  81     1942   1943   2012   -101    -60    -82       C  
ATOM    482  CD2 TYR A  81      46.657  60.596  56.045  1.00 16.94           C  
ANISOU  482  CD2 TYR A  81     2126   2118   2191   -128    -56    -79       C  
ATOM    483  CE1 TYR A  81      45.274  60.240  58.369  1.00 17.46           C  
ANISOU  483  CE1 TYR A  81     2206   2175   2253   -106    -63    -87       C  
ATOM    484  CE2 TYR A  81      46.302  61.691  56.821  1.00 19.39           C  
ANISOU  484  CE2 TYR A  81     2456   2412   2498   -133    -59    -83       C  
ATOM    485  CZ  TYR A  81      45.619  61.482  57.973  1.00 19.46           C  
ANISOU  485  CZ  TYR A  81     2472   2418   2505   -121    -62    -87       C  
ATOM    486  OH  TYR A  81      45.284  62.602  58.761  1.00 22.39           O  
ANISOU  486  OH  TYR A  81     2863   2773   2872   -125    -65    -92       O  
ATOM    487  N   CYS A  82      48.662  55.684  55.166  1.00 10.00           N  
ANISOU  487  N   CYS A  82     1173   1301   1327   -100    -49    -75       N  
ATOM    488  CA  CYS A  82      49.384  54.750  54.310  1.00 10.03           C  
ANISOU  488  CA  CYS A  82     1159   1317   1333    -96    -43    -73       C  
ATOM    489  C   CYS A  82      49.084  53.278  54.698  1.00  9.86           C  
ANISOU  489  C   CYS A  82     1129   1301   1318    -78    -42    -74       C  
ATOM    490  O   CYS A  82      48.948  52.431  53.808  1.00  9.62           O  
ANISOU  490  O   CYS A  82     1094   1273   1291    -69    -35    -74       O  
ATOM    491  CB  CYS A  82      50.875  54.988  54.398  1.00 10.77           C  
ANISOU  491  CB  CYS A  82     1238   1427   1428   -110    -45    -72       C  
ATOM    492  SG  CYS A  82      51.436  56.481  53.543  1.00 12.31           S  
ANISOU  492  SG  CYS A  82     1440   1620   1619   -133    -42    -70       S  
ATOM    493  N   GLN A  83      48.925  52.988  56.003  1.00 10.25           N  
ANISOU  493  N   GLN A  83     1179   1350   1368    -72    -49    -74       N  
ATOM    494  CA AGLN A  83      48.573  51.636  56.437  0.50 10.25           C  
ANISOU  494  CA AGLN A  83     1171   1351   1372    -54    -48    -73       C  
ATOM    495  CA BGLN A  83      48.547  51.640  56.473  0.50 10.15           C  
ANISOU  495  CA BGLN A  83     1158   1338   1359    -54    -48    -73       C  
ATOM    496  C   GLN A  83      47.205  51.268  55.831  1.00  9.63           C  
ANISOU  496  C   GLN A  83     1103   1259   1295    -45    -43    -74       C  
ATOM    497  O   GLN A  83      47.024  50.158  55.295  1.00  9.01           O  
ANISOU  497  O   GLN A  83     1019   1182   1222    -34    -37    -75       O  
ATOM    498  CB AGLN A  83      48.506  51.543  57.974  0.50 10.70           C  
ANISOU  498  CB AGLN A  83     1229   1409   1427    -50    -55    -72       C  
ATOM    499  CB BGLN A  83      48.326  51.590  58.006  0.50 10.39           C  
ANISOU  499  CB BGLN A  83     1193   1369   1388    -50    -56    -73       C  
ATOM    500  CG AGLN A  83      49.862  51.639  58.657  0.50 11.80           C  
ANISOU  500  CG AGLN A  83     1355   1565   1565    -58    -61    -71       C  
ATOM    501  CG BGLN A  83      49.518  51.856  58.902  0.50 11.29           C  
ANISOU  501  CG BGLN A  83     1296   1496   1499    -58    -63    -72       C  
ATOM    502  CD AGLN A  83      49.723  51.897  60.137  0.50 13.07           C  
ANISOU  502  CD AGLN A  83     1520   1726   1720    -58    -71    -71       C  
ATOM    503  CD BGLN A  83      49.210  51.481  60.347  0.50 12.15           C  
ANISOU  503  CD BGLN A  83     1406   1606   1605    -49    -70    -70       C  
ATOM    504  OE1AGLN A  83      50.701  51.816  60.900  0.50 14.13           O  
ANISOU  504  OE1AGLN A  83     1643   1875   1852    -61    -77    -70       O  
ATOM    505  OE1BGLN A  83      48.619  50.434  60.617  0.50 13.99           O  
ANISOU  505  OE1BGLN A  83     1637   1836   1842    -34    -67    -67       O  
ATOM    506  NE2AGLN A  83      48.526  52.256  60.554  0.50 12.53           N  
ANISOU  506  NE2AGLN A  83     1468   1643   1648    -53    -71    -73       N  
ATOM    507  NE2BGLN A  83      49.581  52.350  61.276  0.50 12.28           N  
ANISOU  507  NE2BGLN A  83     1426   1625   1613    -60    -78    -73       N  
ATOM    508  N   ARG A  84      46.254  52.192  55.885  1.00  9.97           N  
ANISOU  508  N   ARG A  84     1163   1291   1335    -48    -45    -75       N  
ATOM    509  CA  ARG A  84      44.866  51.878  55.418  1.00 10.39           C  
ANISOU  509  CA  ARG A  84     1225   1333   1389    -38    -41    -75       C  
ATOM    510  C   ARG A  84      44.840  51.693  53.915  1.00  9.05           C  
ANISOU  510  C   ARG A  84     1054   1165   1220    -40    -35    -75       C  
ATOM    511  O   ARG A  84      44.110  50.866  53.377  1.00  8.52           O  
ANISOU  511  O   ARG A  84      986   1095   1155    -32    -32    -76       O  
ATOM    512  CB  ARG A  84      43.912  52.978  55.834  1.00 11.84           C  
ANISOU  512  CB  ARG A  84     1425   1506   1569    -40    -44    -74       C  
ATOM    513  CG  ARG A  84      43.796  53.036  57.361  1.00 14.66           C  
ANISOU  513  CG  ARG A  84     1785   1861   1924    -36    -50    -74       C  
ATOM    514  CD  ARG A  84      42.651  53.852  57.805  1.00 19.26           C  
ANISOU  514  CD  ARG A  84     2384   2432   2503    -33    -51    -74       C  
ATOM    515  NE  ARG A  84      42.793  54.077  59.243  1.00 22.94           N  
ANISOU  515  NE  ARG A  84     2853   2899   2965    -32    -56    -75       N  
ATOM    516  CZ  ARG A  84      42.123  55.007  59.913  1.00 31.11           C  
ANISOU  516  CZ  ARG A  84     3902   3924   3994    -32    -57    -76       C  
ATOM    517  NH1 ARG A  84      41.191  55.738  59.293  1.00 33.17           N  
ANISOU  517  NH1 ARG A  84     4175   4173   4254    -30    -54    -75       N  
ATOM    518  NH2 ARG A  84      42.392  55.202  61.201  1.00 35.05           N  
ANISOU  518  NH2 ARG A  84     4404   4425   4487    -32    -62    -79       N  
ATOM    519  N   THR A  85      45.667  52.475  53.222  1.00  9.00           N  
ANISOU  519  N   THR A  85     1046   1164   1210    -52    -33    -75       N  
ATOM    520  CA  THR A  85      45.755  52.413  51.762  1.00  8.75           C  
ANISOU  520  CA  THR A  85     1013   1136   1177    -55    -27    -76       C  
ATOM    521  C   THR A  85      46.374  51.107  51.307  1.00  8.59           C  
ANISOU  521  C   THR A  85      979   1125   1161    -48    -22    -78       C  
ATOM    522  O   THR A  85      45.864  50.433  50.392  1.00  8.09           O  
ANISOU  522  O   THR A  85      916   1060   1097    -43    -17    -81       O  
ATOM    523  CB  THR A  85      46.525  53.619  51.187  1.00  9.16           C  
ANISOU  523  CB  THR A  85     1067   1190   1223    -71    -26    -73       C  
ATOM    524  OG1 THR A  85      45.905  54.833  51.632  1.00  8.53           O  
ANISOU  524  OG1 THR A  85     1002   1098   1140    -77    -30    -71       O  
ATOM    525  CG2 THR A  85      46.593  53.596  49.682  1.00  9.06           C  
ANISOU  525  CG2 THR A  85     1053   1181   1206    -74    -19    -72       C  
ATOM    526  N   LEU A  86      47.477  50.742  51.951  1.00  8.80           N  
ANISOU  526  N   LEU A  86      992   1160   1190    -49    -22    -78       N  
ATOM    527  CA  LEU A  86      48.122  49.475  51.614  1.00  8.84           C  
ANISOU  527  CA  LEU A  86      983   1174   1200    -39    -17    -80       C  
ATOM    528  C   LEU A  86      47.192  48.289  51.904  1.00  8.66           C  
ANISOU  528  C   LEU A  86      964   1144   1184    -25    -16    -83       C  
ATOM    529  O   LEU A  86      47.176  47.350  51.136  1.00  9.30           O  
ANISOU  529  O   LEU A  86     1041   1225   1268    -18    -10    -86       O  
ATOM    530  CB  LEU A  86      49.460  49.326  52.301  1.00  9.16           C  
ANISOU  530  CB  LEU A  86     1010   1228   1244    -41    -18    -78       C  
ATOM    531  CG  LEU A  86      50.243  48.043  52.003  1.00  9.40           C  
ANISOU  531  CG  LEU A  86     1025   1268   1280    -30    -11    -79       C  
ATOM    532  CD1 LEU A  86      50.694  47.969  50.552  1.00  9.51           C  
ANISOU  532  CD1 LEU A  86     1035   1288   1291    -32     -1    -82       C  
ATOM    533  CD2 LEU A  86      51.443  47.992  52.973  1.00  9.63           C  
ANISOU  533  CD2 LEU A  86     1038   1310   1312    -30    -15    -75       C  
ATOM    534  N   ARG A  87      46.494  48.311  53.021  1.00  8.55           N  
ANISOU  534  N   ARG A  87      955   1121   1171    -21    -22    -80       N  
ATOM    535  CA  ARG A  87      45.635  47.198  53.425  1.00  8.28           C  
ANISOU  535  CA  ARG A  87      922   1079   1143     -8    -22    -81       C  
ATOM    536  C   ARG A  87      44.509  47.020  52.403  1.00  7.91           C  
ANISOU  536  C   ARG A  87      885   1025   1096     -7    -19    -84       C  
ATOM    537  O   ARG A  87      44.216  45.879  51.946  1.00  8.46           O  
ANISOU  537  O   ARG A  87      953   1092   1171      0    -14    -88       O  
ATOM    538  CB  ARG A  87      45.081  47.489  54.824  1.00  8.74           C  
ANISOU  538  CB  ARG A  87      986   1133   1201     -5    -29    -76       C  
ATOM    539  CG  ARG A  87      44.323  46.316  55.431  1.00  8.25           C  
ANISOU  539  CG  ARG A  87      923   1064   1146      7    -28    -75       C  
ATOM    540  CD  ARG A  87      45.077  44.990  55.486  1.00  8.40           C  
ANISOU  540  CD  ARG A  87      931   1087   1173     17    -24    -75       C  
ATOM    541  NE  ARG A  87      46.458  45.128  55.933  1.00  8.42           N  
ANISOU  541  NE  ARG A  87      922   1102   1175     15    -26    -72       N  
ATOM    542  CZ  ARG A  87      46.860  44.936  57.169  1.00  8.98           C  
ANISOU  542  CZ  ARG A  87      987   1177   1246     20    -30    -66       C  
ATOM    543  NH1 ARG A  87      46.002  44.703  58.141  1.00  9.40           N  
ANISOU  543  NH1 ARG A  87     1047   1225   1301     26    -34    -63       N  
ATOM    544  NH2 ARG A  87      48.134  45.010  57.453  1.00  9.27           N  
ANISOU  544  NH2 ARG A  87     1011   1227   1282     19    -32    -64       N  
ATOM    545  N   GLU A  88      43.843  48.112  52.034  1.00  7.98           N  
ANISOU  545  N   GLU A  88      903   1029   1097    -15    -21    -83       N  
ATOM    546  CA  GLU A  88      42.785  48.117  51.019  1.00  8.14           C  
ANISOU  546  CA  GLU A  88      932   1046   1116    -15    -20    -85       C  
ATOM    547  C   GLU A  88      43.296  47.493  49.719  1.00  8.08           C  
ANISOU  547  C   GLU A  88      920   1044   1107    -16    -13    -91       C  
ATOM    548  O   GLU A  88      42.661  46.579  49.164  1.00  7.97           O  
ANISOU  548  O   GLU A  88      906   1027   1095    -11    -10    -95       O  
ATOM    549  CB  GLU A  88      42.380  49.562  50.685  1.00  8.61           C  
ANISOU  549  CB  GLU A  88     1002   1103   1168    -24    -22    -82       C  
ATOM    550  CG  GLU A  88      41.426  49.728  49.499  1.00  9.34           C  
ANISOU  550  CG  GLU A  88     1100   1193   1254    -25    -21    -82       C  
ATOM    551  CD  GLU A  88      39.970  49.521  49.839  1.00  9.32           C  
ANISOU  551  CD  GLU A  88     1104   1183   1254    -18    -25    -80       C  
ATOM    552  OE1 GLU A  88      39.647  48.994  50.961  1.00 10.32           O  
ANISOU  552  OE1 GLU A  88     1228   1305   1387    -12    -27    -79       O  
ATOM    553  OE2 GLU A  88      39.151  49.838  48.986  1.00 10.74           O  
ANISOU  553  OE2 GLU A  88     1288   1362   1428    -20    -25    -79       O  
ATOM    554  N   ILE A  89      44.444  47.941  49.223  1.00  8.26           N  
ANISOU  554  N   ILE A  89      937   1076   1126    -22     -9    -91       N  
ATOM    555  CA  ILE A  89      44.971  47.464  47.991  1.00  8.77           C  
ANISOU  555  CA  ILE A  89      997   1147   1187    -23     -2    -96       C  
ATOM    556  C   ILE A  89      45.360  45.979  48.084  1.00  8.27           C  
ANISOU  556  C   ILE A  89      926   1085   1132    -12      3   -102       C  
ATOM    557  O   ILE A  89      45.040  45.182  47.209  1.00  9.03           O  
ANISOU  557  O   ILE A  89     1023   1179   1227     -8      8   -109       O  
ATOM    558  CB  ILE A  89      46.169  48.333  47.534  1.00  9.20           C  
ANISOU  558  CB  ILE A  89     1047   1214   1237    -33      2    -93       C  
ATOM    559  CG1 ILE A  89      45.649  49.728  47.186  1.00  9.32           C  
ANISOU  559  CG1 ILE A  89     1072   1225   1243    -43     -2    -88       C  
ATOM    560  CG2 ILE A  89      46.892  47.688  46.366  1.00 10.14           C  
ANISOU  560  CG2 ILE A  89     1159   1342   1353    -31     11    -99       C  
ATOM    561  CD1 ILE A  89      46.752  50.742  46.962  1.00  9.62           C  
ANISOU  561  CD1 ILE A  89     1106   1271   1277    -55      0    -84       C  
ATOM    562  N   GLN A  90      46.140  45.628  49.096  1.00  8.73           N  
ANISOU  562  N   GLN A  90      975   1146   1197     -7      3    -99       N  
ATOM    563  CA  GLN A  90      46.672  44.283  49.165  1.00  9.02           C  
ANISOU  563  CA  GLN A  90     1003   1182   1241      5      9   -102       C  
ATOM    564  C   GLN A  90      45.544  43.244  49.230  1.00  8.80           C  
ANISOU  564  C   GLN A  90      983   1142   1220     12      8   -106       C  
ATOM    565  O   GLN A  90      45.586  42.205  48.597  1.00  9.69           O  
ANISOU  565  O   GLN A  90     1094   1251   1336     19     15   -113       O  
ATOM    566  CB  GLN A  90      47.638  44.106  50.313  1.00  9.12           C  
ANISOU  566  CB  GLN A  90     1004   1200   1260     10      7    -97       C  
ATOM    567  CG  GLN A  90      48.973  44.788  50.097  1.00  9.74           C  
ANISOU  567  CG  GLN A  90     1072   1295   1335      3      9    -94       C  
ATOM    568  CD  GLN A  90      50.054  44.307  50.995  1.00  9.37           C  
ANISOU  568  CD  GLN A  90     1010   1257   1294     10      8    -89       C  
ATOM    569  OE1 GLN A  90      49.972  44.445  52.222  1.00  9.53           O  
ANISOU  569  OE1 GLN A  90     1029   1275   1316     11      0    -84       O  
ATOM    570  NE2 GLN A  90      51.166  43.881  50.397  1.00  9.69           N  
ANISOU  570  NE2 GLN A  90     1038   1308   1336     14     17    -90       N  
ATOM    571  N   ILE A  91      44.507  43.521  50.016  1.00  8.45           N  
ANISOU  571  N   ILE A  91      944   1088   1176     12      1   -102       N  
ATOM    572  CA  ILE A  91      43.357  42.595  50.090  1.00  8.81           C  
ANISOU  572  CA  ILE A  91      997   1123   1229     17      1   -105       C  
ATOM    573  C   ILE A  91      42.567  42.580  48.798  1.00  8.63           C  
ANISOU  573  C   ILE A  91      981   1098   1200     11      2   -112       C  
ATOM    574  O   ILE A  91      42.311  41.508  48.232  1.00  8.27           O  
ANISOU  574  O   ILE A  91      937   1046   1157     15      6   -120       O  
ATOM    575  CB  ILE A  91      42.438  42.934  51.279  1.00  8.72           C  
ANISOU  575  CB  ILE A  91      989   1105   1219     17     -7    -97       C  
ATOM    576  CG1 ILE A  91      43.187  42.654  52.597  1.00  8.46           C  
ANISOU  576  CG1 ILE A  91      950   1074   1193     25     -8    -91       C  
ATOM    577  CG2 ILE A  91      41.143  42.153  51.207  1.00  9.05           C  
ANISOU  577  CG2 ILE A  91     1037   1136   1266     20     -8    -99       C  
ATOM    578  CD1 ILE A  91      42.523  43.116  53.851  1.00  8.62           C  
ANISOU  578  CD1 ILE A  91      973   1091   1213     25    -15    -83       C  
ATOM    579  N   LEU A  92      42.153  43.733  48.299  1.00  8.77           N  
ANISOU  579  N   LEU A  92     1004   1120   1208      2     -2   -110       N  
ATOM    580  CA  LEU A  92      41.245  43.728  47.179  1.00  9.31           C  
ANISOU  580  CA  LEU A  92     1080   1188   1270     -2     -2   -115       C  
ATOM    581  C   LEU A  92      41.861  43.275  45.866  1.00 10.41           C  
ANISOU  581  C   LEU A  92     1218   1333   1403     -4      6   -124       C  
ATOM    582  O   LEU A  92      41.181  42.648  45.058  1.00 11.70           O  
ANISOU  582  O   LEU A  92     1386   1494   1565     -5      6   -132       O  
ATOM    583  CB  LEU A  92      40.556  45.082  47.000  1.00  9.34           C  
ANISOU  583  CB  LEU A  92     1089   1194   1265    -10     -8   -109       C  
ATOM    584  CG  LEU A  92      39.584  45.428  48.126  1.00  9.63           C  
ANISOU  584  CG  LEU A  92     1129   1223   1306     -7    -14   -101       C  
ATOM    585  CD1 LEU A  92      38.931  46.732  47.785  1.00 11.04           C  
ANISOU  585  CD1 LEU A  92     1315   1404   1476    -13    -19    -95       C  
ATOM    586  CD2 LEU A  92      38.561  44.350  48.361  1.00  9.79           C  
ANISOU  586  CD2 LEU A  92     1150   1236   1333     -3    -16   -104       C  
ATOM    587  N   LEU A  93      43.161  43.474  45.679  1.00 10.14           N  
ANISOU  587  N   LEU A  93     1177   1308   1367     -3     11   -124       N  
ATOM    588  CA  LEU A  93      43.779  42.884  44.514  1.00 11.41           C  
ANISOU  588  CA  LEU A  93     1336   1474   1523     -2     20   -134       C  
ATOM    589  C   LEU A  93      43.796  41.385  44.514  1.00 12.53           C  
ANISOU  589  C   LEU A  93     1478   1609   1675      7     26   -143       C  
ATOM    590  O   LEU A  93      43.935  40.826  43.415  1.00 16.39           O  
ANISOU  590  O   LEU A  93     1969   2099   2158      7     32   -153       O  
ATOM    591  CB  LEU A  93      45.245  43.376  44.416  1.00 11.11           C  
ANISOU  591  CB  LEU A  93     1290   1449   1484     -3     26   -131       C  
ATOM    592  CG  LEU A  93      45.451  44.835  43.985  1.00 12.30           C  
ANISOU  592  CG  LEU A  93     1442   1609   1624    -14     24   -124       C  
ATOM    593  CD1 LEU A  93      46.917  45.139  43.868  1.00 12.37           C  
ANISOU  593  CD1 LEU A  93     1439   1630   1630    -16     31   -121       C  
ATOM    594  CD2 LEU A  93      44.783  45.169  42.676  1.00 13.74           C  
ANISOU  594  CD2 LEU A  93     1632   1795   1793    -21     25   -127       C  
ATOM    595  N  AARG A  94      43.660  40.726  45.649  0.50 11.43           N  
ANISOU  595  N  AARG A  94     1337   1460   1548     14     23   -139       N  
ATOM    596  N  BARG A  94      43.680  40.741  45.694  0.50 11.92           N  
ANISOU  596  N  BARG A  94     1398   1521   1610     15     23   -139       N  
ATOM    597  CA AARG A  94      43.728  39.276  45.700  0.50 10.94           C  
ANISOU  597  CA AARG A  94     1274   1386   1495     24     29   -147       C  
ATOM    598  CA BARG A  94      43.824  39.264  45.899  0.50 11.60           C  
ANISOU  598  CA BARG A  94     1357   1470   1581     25     29   -146       C  
ATOM    599  C  AARG A  94      42.319  38.674  45.697  0.50 10.40           C  
ANISOU  599  C  AARG A  94     1215   1305   1431     21     24   -151       C  
ATOM    600  C  BARG A  94      42.515  38.590  46.291  0.50 11.55           C  
ANISOU  600  C  BARG A  94     1358   1449   1581     25     24   -147       C  
ATOM    601  O  AARG A  94      42.047  37.690  44.990  0.50 10.27           O  
ANISOU  601  O  AARG A  94     1204   1282   1416     22     29   -162       O  
ATOM    602  O  BARG A  94      42.471  37.380  46.554  0.50 12.37           O  
ANISOU  602  O  BARG A  94     1463   1541   1696     32     28   -151       O  
ATOM    603  CB AARG A  94      44.589  38.865  46.880  0.50 10.67           C  
ANISOU  603  CB AARG A  94     1230   1350   1472     35     31   -140       C  
ATOM    604  CB BARG A  94      44.874  38.979  46.948  0.50 11.53           C  
ANISOU  604  CB BARG A  94     1338   1463   1581     35     32   -138       C  
ATOM    605  CG AARG A  94      46.079  39.264  46.667  0.50 10.79           C  
ANISOU  605  CG AARG A  94     1235   1381   1484     37     37   -138       C  
ATOM    606  CG BARG A  94      46.253  39.557  46.603  0.50 11.50           C  
ANISOU  606  CG BARG A  94     1323   1474   1572     36     37   -137       C  
ATOM    607  CD AARG A  94      46.901  39.260  47.936  0.50 10.36           C  
ANISOU  607  CD AARG A  94     1169   1329   1437     45     36   -127       C  
ATOM    608  CD BARG A  94      47.168  39.443  47.776  0.50 11.14           C  
ANISOU  608  CD BARG A  94     1267   1432   1535     44     37   -127       C  
ATOM    609  NE AARG A  94      48.352  39.445  47.715  0.50 10.23           N  
ANISOU  609  NE AARG A  94     1141   1328   1420     48     42   -126       N  
ATOM    610  NE BARG A  94      48.564  39.712  47.430  0.50 11.03           N  
ANISOU  610  NE BARG A  94     1240   1433   1517     46     43   -126       N  
ATOM    611  CZ AARG A  94      48.967  40.630  47.639  0.50  9.98           C  
ANISOU  611  CZ AARG A  94     1102   1310   1380     39     40   -120       C  
ATOM    612  CZ BARG A  94      49.031  40.908  47.090  0.50 10.95           C  
ANISOU  612  CZ BARG A  94     1226   1436   1497     35     42   -123       C  
ATOM    613  NH1AARG A  94      48.286  41.758  47.759  0.50  9.64           N  
ANISOU  613  NH1AARG A  94     1066   1267   1329     26     31   -117       N  
ATOM    614  NH1BARG A  94      48.221  41.943  47.019  0.50 10.63           N  
ANISOU  614  NH1BARG A  94     1194   1394   1449     22     34   -120       N  
ATOM    615  NH2AARG A  94      50.266  40.695  47.430  0.50 10.00           N  
ANISOU  615  NH2AARG A  94     1091   1326   1381     42     46   -119       N  
ATOM    616  NH2BARG A  94      50.310  41.075  46.826  0.50 10.88           N  
ANISOU  616  NH2BARG A  94     1204   1442   1486     36     48   -121       N  
ATOM    617  N  APHE A  95      41.433  39.231  46.514  0.50  9.59           N  
ANISOU  617  N  APHE A  95     1114   1200   1330     17     16   -142       N  
ATOM    618  N  BPHE A  95      41.444  39.368  46.271  0.50 10.47           N  
ANISOU  618  N  BPHE A  95     1226   1313   1439     16     16   -143       N  
ATOM    619  CA APHE A  95      40.038  38.745  46.573  0.50  9.53           C  
ANISOU  619  CA APHE A  95     1113   1183   1326     13     10   -144       C  
ATOM    620  CA BPHE A  95      40.083  38.854  46.475  0.50 10.25           C  
ANISOU  620  CA BPHE A  95     1204   1275   1416     13     10   -144       C  
ATOM    621  C  APHE A  95      39.360  38.846  45.185  0.50  9.75           C  
ANISOU  621  C  APHE A  95     1147   1214   1342      4      9   -153       C  
ATOM    622  C  BPHE A  95      39.334  38.881  45.137  0.50 10.14           C  
ANISOU  622  C  BPHE A  95     1196   1264   1391      4      9   -153       C  
ATOM    623  O  APHE A  95      39.551  39.816  44.425  0.50  9.44           O  
ANISOU  623  O  APHE A  95     1108   1187   1291     -1      8   -153       O  
ATOM    624  O  BPHE A  95      39.480  39.821  44.334  0.50  9.69           O  
ANISOU  624  O  BPHE A  95     1141   1219   1322     -2      8   -153       O  
ATOM    625  CB APHE A  95      39.195  39.597  47.524  0.50  9.26           C  
ANISOU  625  CB APHE A  95     1078   1148   1291     11      2   -132       C  
ATOM    626  CB BPHE A  95      39.347  39.752  47.473  0.50 10.04           C  
ANISOU  626  CB BPHE A  95     1177   1249   1390     10      2   -131       C  
ATOM    627  CG APHE A  95      39.343  39.282  48.999  0.50  9.10           C  
ANISOU  627  CG APHE A  95     1054   1122   1283     19      1   -122       C  
ATOM    628  CG BPHE A  95      39.460  39.306  48.906  0.50  9.88           C  
ANISOU  628  CG BPHE A  95     1152   1221   1380     19      1   -123       C  
ATOM    629  CD1APHE A  95      40.026  38.187  49.484  0.50  9.00           C  
ANISOU  629  CD1APHE A  95     1038   1102   1280     28      7   -123       C  
ATOM    630  CD1BPHE A  95      40.247  38.238  49.255  0.50  9.87           C  
ANISOU  630  CD1BPHE A  95     1148   1214   1389     28      8   -125       C  
ATOM    631  CD2APHE A  95      38.744  40.132  49.909  0.50  8.70           C  
ANISOU  631  CD2APHE A  95     1003   1072   1230     17     -6   -112       C  
ATOM    632  CD2BPHE A  95      38.798  40.000  49.915  0.50  9.43           C  
ANISOU  632  CD2BPHE A  95     1095   1164   1324     18     -5   -113       C  
ATOM    633  CE1APHE A  95      40.092  37.953  50.864  0.50  8.90           C  
ANISOU  633  CE1APHE A  95     1021   1084   1276     35      5   -113       C  
ATOM    634  CE1BPHE A  95      40.320  37.806  50.564  0.50  9.88           C  
ANISOU  634  CE1BPHE A  95     1146   1209   1400     35      7   -116       C  
ATOM    635  CE2APHE A  95      38.788  39.881  51.258  0.50  8.81           C  
ANISOU  635  CE2APHE A  95     1014   1081   1252     24     -7   -104       C  
ATOM    636  CE2BPHE A  95      38.890  39.574  51.232  0.50  9.42           C  
ANISOU  636  CE2BPHE A  95     1091   1157   1331     25     -6   -105       C  
ATOM    637  CZ APHE A  95      39.451  38.803  51.737  0.50  8.77           C  
ANISOU  637  CZ APHE A  95     1006   1071   1257     33     -2   -104       C  
ATOM    638  CZ BPHE A  95      39.652  38.481  51.551  0.50  9.58           C  
ANISOU  638  CZ BPHE A  95     1107   1171   1360     34      0   -106       C  
ATOM    639  N   ARG A  96      38.507  37.872  44.906  1.00 10.23           N  
ANISOU  639  N   ARG A  96     1213   1265   1408      1      8   -161       N  
ATOM    640  CA  ARG A  96      37.613  37.911  43.760  1.00 10.95           C  
ANISOU  640  CA  ARG A  96     1311   1361   1490     -9      4   -169       C  
ATOM    641  C   ARG A  96      36.345  37.167  44.144  1.00  9.95           C  
ANISOU  641  C   ARG A  96     1186   1223   1371    -13     -1   -170       C  
ATOM    642  O   ARG A  96      36.338  35.930  44.295  1.00 11.01           O  
ANISOU  642  O   ARG A  96     1322   1344   1516    -11      3   -177       O  
ATOM    643  CB  ARG A  96      38.265  37.278  42.567  1.00 14.04           C  
ANISOU  643  CB  ARG A  96     1706   1754   1875     -9     12   -184       C  
ATOM    644  CG  ARG A  96      37.408  37.339  41.305  1.00 18.58           C  
ANISOU  644  CG  ARG A  96     2287   2336   2436    -20      7   -194       C  
ATOM    645  CD  ARG A  96      38.162  36.576  40.226  1.00 23.70           C  
ANISOU  645  CD  ARG A  96     2940   2984   3078    -18     17   -210       C  
ATOM    646  NE  ARG A  96      37.499  36.603  38.950  1.00 30.89           N  
ANISOU  646  NE  ARG A  96     3858   3904   3974    -29     13   -221       N  
ATOM    647  CZ  ARG A  96      37.993  36.037  37.845  1.00 37.65           C  
ANISOU  647  CZ  ARG A  96     4721   4763   4821    -29     21   -237       C  
ATOM    648  NH1 ARG A  96      39.199  35.430  37.867  1.00 37.33           N  
ANISOU  648  NH1 ARG A  96     4679   4717   4785    -18     33   -243       N  
ATOM    649  NH2 ARG A  96      37.283  36.074  36.718  1.00 39.15           N  
ANISOU  649  NH2 ARG A  96     4917   4963   4996    -40     15   -246       N  
ATOM    650  N   HIS A  97      35.270  37.927  44.342  1.00  9.42           N  
ANISOU  650  N   HIS A  97     1117   1161   1301    -19    -10   -161       N  
ATOM    651  CA  HIS A  97      34.002  37.355  44.770  1.00  9.09           C  
ANISOU  651  CA  HIS A  97     1076   1112   1267    -24    -16   -159       C  
ATOM    652  C   HIS A  97      32.882  38.283  44.358  1.00  8.94           C  
ANISOU  652  C   HIS A  97     1055   1104   1238    -31    -25   -153       C  
ATOM    653  O   HIS A  97      32.996  39.504  44.433  1.00  8.69           O  
ANISOU  653  O   HIS A  97     1022   1083   1199    -29    -28   -144       O  
ATOM    654  CB  HIS A  97      34.031  37.125  46.302  1.00  8.44           C  
ANISOU  654  CB  HIS A  97      989   1020   1199    -16    -15   -147       C  
ATOM    655  CG  HIS A  97      32.848  36.417  46.829  1.00  8.35           C  
ANISOU  655  CG  HIS A  97      977   1000   1197    -20    -18   -144       C  
ATOM    656  ND1 HIS A  97      31.635  37.031  47.049  1.00  8.66           N  
ANISOU  656  ND1 HIS A  97     1012   1044   1233    -26    -26   -136       N  
ATOM    657  CD2 HIS A  97      32.672  35.122  47.141  1.00  8.23           C  
ANISOU  657  CD2 HIS A  97      964    970   1195    -21    -15   -149       C  
ATOM    658  CE1 HIS A  97      30.762  36.155  47.469  1.00  8.44           C  
ANISOU  658  CE1 HIS A  97      983   1008   1215    -30    -28   -134       C  
ATOM    659  NE2 HIS A  97      31.371  34.979  47.547  1.00  8.31           N  
ANISOU  659  NE2 HIS A  97      971    978   1209    -28    -21   -142       N  
ATOM    660  N   GLU A  98      31.749  37.700  43.967  1.00  8.99           N  
ANISOU  660  N   GLU A  98     1062   1110   1245    -41    -31   -158       N  
ATOM    661  CA  GLU A  98      30.604  38.475  43.531  1.00  9.49           C  
ANISOU  661  CA  GLU A  98     1123   1185   1299    -47    -40   -152       C  
ATOM    662  C   GLU A  98      30.095  39.503  44.540  1.00  8.92           C  
ANISOU  662  C   GLU A  98     1044   1115   1228    -41    -44   -134       C  
ATOM    663  O   GLU A  98      29.522  40.529  44.158  1.00  9.80           O  
ANISOU  663  O   GLU A  98     1154   1239   1330    -43    -50   -127       O  
ATOM    664  CB  GLU A  98      29.429  37.574  43.155  1.00 10.55           C  
ANISOU  664  CB  GLU A  98     1255   1316   1436    -59    -46   -158       C  
ATOM    665  CG  GLU A  98      29.638  36.755  41.922  1.00 13.29           C  
ANISOU  665  CG  GLU A  98     1610   1664   1777    -68    -45   -177       C  
ATOM    666  CD  GLU A  98      28.480  35.891  41.579  1.00 16.72           C  
ANISOU  666  CD  GLU A  98     2043   2096   2214    -81    -52   -184       C  
ATOM    667  OE1 GLU A  98      27.606  35.576  42.465  1.00 17.86           O  
ANISOU  667  OE1 GLU A  98     2181   2234   2370    -83    -55   -175       O  
ATOM    668  OE2 GLU A  98      28.522  35.435  40.383  1.00 22.68           O  
ANISOU  668  OE2 GLU A  98     2804   2854   2959    -90    -54   -199       O  
ATOM    669  N   ASN A  99      30.244  39.206  45.833  1.00  8.44           N  
ANISOU  669  N   ASN A  99      981   1044   1180    -34    -40   -127       N  
ATOM    670  CA  ASN A  99      29.745  40.096  46.865  1.00  8.10           C  
ANISOU  670  CA  ASN A  99      934   1005   1140    -28    -43   -112       C  
ATOM    671  C   ASN A  99      30.824  40.926  47.548  1.00  7.58           C  
ANISOU  671  C   ASN A  99      870    938   1072    -19    -38   -107       C  
ATOM    672  O   ASN A  99      30.584  41.456  48.642  1.00  7.32           O  
ANISOU  672  O   ASN A  99      835    904   1043    -13    -39    -96       O  
ATOM    673  CB  ASN A  99      28.921  39.309  47.881  1.00  8.03           C  
ANISOU  673  CB  ASN A  99      920    986   1143    -28    -43   -107       C  
ATOM    674  CG  ASN A  99      27.770  38.559  47.256  1.00  8.22           C  
ANISOU  674  CG  ASN A  99      942   1013   1170    -40    -48   -111       C  
ATOM    675  OD1 ASN A  99      27.751  37.327  47.285  1.00  8.50           O  
ANISOU  675  OD1 ASN A  99      978   1037   1215    -45    -46   -119       O  
ATOM    676  ND2 ASN A  99      26.866  39.284  46.595  1.00  8.30           N  
ANISOU  676  ND2 ASN A  99      948   1036   1170    -44    -56   -108       N  
ATOM    677  N   VAL A 100      31.969  41.092  46.884  1.00  7.73           N  
ANISOU  677  N   VAL A 100      892    959   1085    -19    -34   -114       N  
ATOM    678  CA  VAL A 100      33.077  41.933  47.367  1.00  7.64           C  
ANISOU  678  CA  VAL A 100      882    950   1071    -12    -31   -109       C  
ATOM    679  C   VAL A 100      33.496  42.844  46.200  1.00  7.96           C  
ANISOU  679  C   VAL A 100      926   1001   1098    -16    -31   -112       C  
ATOM    680  O   VAL A 100      33.694  42.359  45.087  1.00  8.86           O  
ANISOU  680  O   VAL A 100     1042   1118   1206    -21    -30   -122       O  
ATOM    681  CB  VAL A 100      34.245  41.065  47.887  1.00  7.88           C  
ANISOU  681  CB  VAL A 100      912    973   1110     -7    -24   -114       C  
ATOM    682  CG1 VAL A 100      35.367  41.982  48.372  1.00  8.32           C  
ANISOU  682  CG1 VAL A 100      966   1033   1162     -2    -22   -109       C  
ATOM    683  CG2 VAL A 100      33.824  40.157  49.012  1.00  7.90           C  
ANISOU  683  CG2 VAL A 100      911    964   1125     -3    -23   -110       C  
ATOM    684  N   ILE A 101      33.642  44.142  46.435  1.00  8.00           N  
ANISOU  684  N   ILE A 101      933   1011   1097    -15    -33   -103       N  
ATOM    685  CA  ILE A 101      34.049  45.017  45.341  1.00  8.35           C  
ANISOU  685  CA  ILE A 101      980   1064   1128    -19    -33   -104       C  
ATOM    686  C   ILE A 101      35.466  44.639  44.918  1.00  8.36           C  
ANISOU  686  C   ILE A 101      981   1066   1128    -20    -26   -112       C  
ATOM    687  O   ILE A 101      36.323  44.351  45.746  1.00  8.93           O  
ANISOU  687  O   ILE A 101     1050   1133   1208    -15    -22   -112       O  
ATOM    688  CB  ILE A 101      33.942  46.493  45.783  1.00  8.23           C  
ANISOU  688  CB  ILE A 101      969   1051   1109    -17    -35    -92       C  
ATOM    689  CG1 ILE A 101      33.931  47.492  44.595  1.00  8.85           C  
ANISOU  689  CG1 ILE A 101     1051   1137   1174    -21    -36    -89       C  
ATOM    690  CG2 ILE A 101      34.949  46.847  46.854  1.00  8.29           C  
ANISOU  690  CG2 ILE A 101      976   1053   1122    -13    -32    -89       C  
ATOM    691  CD1 ILE A 101      32.754  47.334  43.637  1.00  8.83           C  
ANISOU  691  CD1 ILE A 101     1048   1142   1164    -24    -42    -89       C  
ATOM    692  N   GLY A 102      35.700  44.649  43.612  1.00  8.77           N  
ANISOU  692  N   GLY A 102     1036   1127   1170    -25    -24   -118       N  
ATOM    693  CA  GLY A 102      37.017  44.386  43.094  1.00  9.38           C  
ANISOU  693  CA  GLY A 102     1111   1207   1244    -25    -16   -125       C  
ATOM    694  C   GLY A 102      37.804  45.634  42.802  1.00  8.63           C  
ANISOU  694  C   GLY A 102     1018   1120   1141    -27    -14   -119       C  
ATOM    695  O   GLY A 102      37.324  46.754  42.991  1.00  9.56           O  
ANISOU  695  O   GLY A 102     1139   1239   1255    -29    -19   -108       O  
ATOM    696  N   ILE A 103      39.025  45.468  42.318  1.00  9.35           N  
ANISOU  696  N   ILE A 103     1106   1216   1229    -28     -6   -124       N  
ATOM    697  CA  ILE A 103      39.809  46.555  41.726  1.00  9.68           C  
ANISOU  697  CA  ILE A 103     1150   1268   1262    -33     -3   -118       C  
ATOM    698  C   ILE A 103      40.024  46.255  40.247  1.00  9.84           C  
ANISOU  698  C   ILE A 103     1171   1298   1268    -37      2   -126       C  
ATOM    699  O   ILE A 103      40.633  45.199  39.908  1.00 11.58           O  
ANISOU  699  O   ILE A 103     1389   1520   1491    -33      9   -138       O  
ATOM    700  CB  ILE A 103      41.147  46.809  42.455  1.00  9.73           C  
ANISOU  700  CB  ILE A 103     1150   1274   1274    -32      2   -115       C  
ATOM    701  CG1 ILE A 103      40.865  47.362  43.851  1.00  9.19           C  
ANISOU  701  CG1 ILE A 103     1080   1197   1213    -29     -4   -107       C  
ATOM    702  CG2 ILE A 103      42.038  47.734  41.646  1.00  9.90           C  
ANISOU  702  CG2 ILE A 103     1170   1306   1284    -38      7   -112       C  
ATOM    703  CD1 ILE A 103      42.086  47.544  44.750  1.00  9.84           C  
ANISOU  703  CD1 ILE A 103     1156   1280   1302    -29     -1   -104       C  
ATOM    704  N   ARG A 104      39.615  47.186  39.379  1.00 10.77           N  
ANISOU  704  N   ARG A 104     1294   1424   1373    -42     -1   -120       N  
ATOM    705  CA  ARG A 104      39.764  47.022  37.939  1.00 11.85           C  
ANISOU  705  CA  ARG A 104     1434   1573   1495    -46      3   -127       C  
ATOM    706  C   ARG A 104      41.087  47.587  37.405  1.00 11.79           C  
ANISOU  706  C   ARG A 104     1425   1576   1481    -49     13   -124       C  
ATOM    707  O   ARG A 104      41.584  47.123  36.398  1.00 11.87           O  
ANISOU  707  O   ARG A 104     1435   1595   1482    -50     20   -132       O  
ATOM    708  CB  ARG A 104      38.637  47.764  37.216  1.00 12.64           C  
ANISOU  708  CB  ARG A 104     1540   1678   1583    -51     -5   -120       C  
ATOM    709  CG  ARG A 104      37.191  47.282  37.488  1.00 14.61           C  
ANISOU  709  CG  ARG A 104     1791   1923   1836    -49    -14   -121       C  
ATOM    710  CD  ARG A 104      36.988  45.806  37.402  1.00 19.89           C  
ANISOU  710  CD  ARG A 104     2458   2588   2510    -48    -14   -137       C  
ATOM    711  NE  ARG A 104      37.046  45.379  36.035  1.00 22.27           N  
ANISOU  711  NE  ARG A 104     2764   2902   2797    -53    -11   -147       N  
ATOM    712  CZ  ARG A 104      36.011  44.964  35.292  1.00 23.78           C  
ANISOU  712  CZ  ARG A 104     2957   3098   2979    -57    -18   -153       C  
ATOM    713  NH1 ARG A 104      34.774  44.917  35.758  1.00 24.17           N  
ANISOU  713  NH1 ARG A 104     3006   3143   3034    -58    -28   -148       N  
ATOM    714  NH2 ARG A 104      36.257  44.563  34.071  1.00 23.11           N  
ANISOU  714  NH2 ARG A 104     2877   3025   2880    -61    -15   -163       N  
ATOM    715  N   ASP A 105      41.571  48.658  38.018  1.00 10.52           N  
ANISOU  715  N   ASP A 105     1262   1413   1324    -52     12   -112       N  
ATOM    716  CA  ASP A 105      42.776  49.366  37.563  1.00 10.24           C  
ANISOU  716  CA  ASP A 105     1223   1385   1281    -57     21   -107       C  
ATOM    717  C   ASP A 105      43.247  50.270  38.661  1.00  9.68           C  
ANISOU  717  C   ASP A 105     1151   1308   1220    -60     18    -97       C  
ATOM    718  O   ASP A 105      42.450  50.649  39.584  1.00  9.02           O  
ANISOU  718  O   ASP A 105     1070   1213   1143    -58     10    -92       O  
ATOM    719  CB  ASP A 105      42.391  50.254  36.380  1.00 10.28           C  
ANISOU  719  CB  ASP A 105     1235   1400   1269    -64     20   -100       C  
ATOM    720  CG  ASP A 105      43.576  50.740  35.532  1.00 10.80           C  
ANISOU  720  CG  ASP A 105     1298   1479   1325    -70     31    -96       C  
ATOM    721  OD1 ASP A 105      44.706  50.292  35.699  1.00 11.32           O  
ANISOU  721  OD1 ASP A 105     1355   1548   1396    -69     39   -101       O  
ATOM    722  OD2 ASP A 105      43.282  51.621  34.645  1.00 11.15           O  
ANISOU  722  OD2 ASP A 105     1349   1530   1356    -76     30    -87       O  
ATOM    723  N   ILE A 106      44.521  50.624  38.629  1.00  9.63           N  
ANISOU  723  N   ILE A 106     1137   1308   1214    -65     26    -94       N  
ATOM    724  CA  ILE A 106      45.037  51.595  39.553  1.00  9.83           C  
ANISOU  724  CA  ILE A 106     1162   1328   1246    -70     23    -85       C  
ATOM    725  C   ILE A 106      45.967  52.516  38.766  1.00 10.05           C  
ANISOU  725  C   ILE A 106     1188   1366   1265    -81     31    -77       C  
ATOM    726  O   ILE A 106      46.859  52.013  38.023  1.00 10.45           O  
ANISOU  726  O   ILE A 106     1230   1430   1310    -81     40    -82       O  
ATOM    727  CB  ILE A 106      45.804  50.958  40.732  1.00 10.52           C  
ANISOU  727  CB  ILE A 106     1238   1412   1346    -66     24    -89       C  
ATOM    728  CG1 ILE A 106      44.943  49.924  41.506  1.00 10.80           C  
ANISOU  728  CG1 ILE A 106     1274   1437   1391    -55     18    -96       C  
ATOM    729  CG2 ILE A 106      46.356  52.071  41.616  1.00 10.95           C  
ANISOU  729  CG2 ILE A 106     1291   1462   1405    -74     21    -80       C  
ATOM    730  CD1 ILE A 106      45.693  49.215  42.593  1.00 11.39           C  
ANISOU  730  CD1 ILE A 106     1339   1511   1478    -49     19    -99       C  
ATOM    731  N   LEU A 107      45.778  53.829  38.925  1.00 10.23           N  
ANISOU  731  N   LEU A 107     1218   1382   1285    -89     27    -65       N  
ATOM    732  CA  LEU A 107      46.671  54.830  38.280  1.00 10.71           C  
ANISOU  732  CA  LEU A 107     1279   1451   1339   -101     33    -56       C  
ATOM    733  C   LEU A 107      47.524  55.505  39.346  1.00  9.94           C  
ANISOU  733  C   LEU A 107     1177   1348   1252   -110     32    -51       C  
ATOM    734  O   LEU A 107      47.024  55.922  40.405  1.00  9.55           O  
ANISOU  734  O   LEU A 107     1133   1285   1210   -109     24    -50       O  
ATOM    735  CB  LEU A 107      45.892  55.878  37.486  1.00 11.47           C  
ANISOU  735  CB  LEU A 107     1388   1545   1425   -106     31    -45       C  
ATOM    736  CG  LEU A 107      44.968  55.295  36.403  1.00 13.05           C  
ANISOU  736  CG  LEU A 107     1593   1752   1613    -99     31    -49       C  
ATOM    737  CD1 LEU A 107      43.605  54.893  36.971  1.00 14.52           C  
ANISOU  737  CD1 LEU A 107     1785   1927   1804    -89     21    -52       C  
ATOM    738  CD2 LEU A 107      44.787  56.264  35.224  1.00 13.43           C  
ANISOU  738  CD2 LEU A 107     1650   1807   1646   -105     34    -36       C  
ATOM    739  N   ARG A 108      48.787  55.754  39.036  1.00  9.95           N  
ANISOU  739  N   ARG A 108     1169   1361   1252   -119     40    -48       N  
ATOM    740  CA  ARG A 108      49.661  56.546  39.885  1.00 10.25           C  
ANISOU  740  CA  ARG A 108     1201   1395   1297   -131     38    -43       C  
ATOM    741  C   ARG A 108      50.895  56.911  39.044  1.00 10.53           C  
ANISOU  741  C   ARG A 108     1228   1447   1327   -143     49    -37       C  
ATOM    742  O   ARG A 108      51.075  56.370  37.936  1.00 11.26           O  
ANISOU  742  O   ARG A 108     1315   1552   1410   -139     58    -39       O  
ATOM    743  CB  ARG A 108      49.978  55.819  41.217  1.00 10.01           C  
ANISOU  743  CB  ARG A 108     1161   1362   1279   -125     33    -50       C  
ATOM    744  CG  ARG A 108      50.568  54.430  41.147  1.00  9.87           C  
ANISOU  744  CG  ARG A 108     1129   1357   1264   -114     38    -60       C  
ATOM    745  CD  ARG A 108      52.001  54.408  40.601  1.00 10.30           C  
ANISOU  745  CD  ARG A 108     1168   1430   1317   -121     49    -57       C  
ATOM    746  NE  ARG A 108      52.607  53.123  40.817  1.00 10.23           N  
ANISOU  746  NE  ARG A 108     1144   1431   1314   -109     53    -66       N  
ATOM    747  CZ  ARG A 108      53.696  52.702  40.152  1.00 11.02           C  
ANISOU  747  CZ  ARG A 108     1228   1548   1410   -109     65    -66       C  
ATOM    748  NH1 ARG A 108      54.278  53.481  39.233  1.00 11.41           N  
ANISOU  748  NH1 ARG A 108     1276   1608   1451   -121     73    -59       N  
ATOM    749  NH2 ARG A 108      54.223  51.510  40.420  1.00 11.51           N  
ANISOU  749  NH2 ARG A 108     1277   1617   1478    -95     69    -74       N  
ATOM    750  N   ALA A 109      51.683  57.850  39.547  1.00 10.58           N  
ANISOU  750  N   ALA A 109     1231   1451   1337   -158     48    -30       N  
ATOM    751  CA  ALA A 109      52.818  58.349  38.820  1.00 10.77           C  
ANISOU  751  CA  ALA A 109     1246   1489   1357   -172     58    -22       C  
ATOM    752  C   ALA A 109      53.860  57.318  38.554  1.00 11.50           C  
ANISOU  752  C   ALA A 109     1318   1602   1450   -167     67    -28       C  
ATOM    753  O   ALA A 109      53.987  56.362  39.284  1.00 11.20           O  
ANISOU  753  O   ALA A 109     1271   1566   1419   -156     64    -37       O  
ATOM    754  CB  ALA A 109      53.422  59.524  39.564  1.00 10.78           C  
ANISOU  754  CB  ALA A 109     1248   1483   1365   -191     53    -14       C  
ATOM    755  N   SER A 110      54.698  57.575  37.538  1.00 12.20           N  
ANISOU  755  N   SER A 110     1398   1706   1530   -175     78    -21       N  
ATOM    756  CA  SER A 110      55.694  56.565  37.139  1.00 13.38           C  
ANISOU  756  CA  SER A 110     1528   1877   1679   -168     89    -27       C  
ATOM    757  C   SER A 110      56.881  56.472  38.076  1.00 13.57           C  
ANISOU  757  C   SER A 110     1532   1909   1713   -174     88    -26       C  
ATOM    758  O   SER A 110      57.675  55.533  37.957  1.00 15.56           O  
ANISOU  758  O   SER A 110     1767   2179   1968   -165     96    -31       O  
ATOM    759  CB  SER A 110      56.213  56.913  35.754  1.00 14.30           C  
ANISOU  759  CB  SER A 110     1641   2009   1781   -176    103    -19       C  
ATOM    760  OG  SER A 110      56.879  58.146  35.763  1.00 15.59           O  
ANISOU  760  OG  SER A 110     1804   2174   1946   -197    104     -6       O  
ATOM    761  N   THR A 111      57.085  57.482  38.921  1.00 12.64           N  
ANISOU  761  N   THR A 111     1417   1783   1603   -191     80    -20       N  
ATOM    762  CA  THR A 111      58.132  57.432  39.909  1.00 12.96           C  
ANISOU  762  CA  THR A 111     1439   1832   1654   -198     76    -20       C  
ATOM    763  C   THR A 111      57.576  57.618  41.330  1.00 12.90           C  
ANISOU  763  C   THR A 111     1440   1806   1655   -197     60    -24       C  
ATOM    764  O   THR A 111      56.568  58.316  41.546  1.00 12.39           O  
ANISOU  764  O   THR A 111     1396   1722   1590   -200     53    -23       O  
ATOM    765  CB  THR A 111      59.214  58.521  39.682  1.00 13.77           C  
ANISOU  765  CB  THR A 111     1532   1944   1755   -222     80     -8       C  
ATOM    766  OG1 THR A 111      58.614  59.808  39.828  1.00 16.17           O  
ANISOU  766  OG1 THR A 111     1856   2228   2058   -238     73     -1       O  
ATOM    767  CG2 THR A 111      59.812  58.397  38.284  1.00 14.48           C  
ANISOU  767  CG2 THR A 111     1613   2054   1835   -223     97     -2       C  
ATOM    768  N   LEU A 112      58.295  57.087  42.307  1.00 12.63           N  
ANISOU  768  N   LEU A 112     1389   1781   1630   -195     56    -28       N  
ATOM    769  CA  LEU A 112      57.922  57.175  43.693  1.00 13.30           C  
ANISOU  769  CA  LEU A 112     1479   1853   1722   -194     42    -32       C  
ATOM    770  C   LEU A 112      57.845  58.634  44.165  1.00 13.16           C  
ANISOU  770  C   LEU A 112     1474   1821   1704   -217     34    -26       C  
ATOM    771  O   LEU A 112      56.907  59.023  44.863  1.00 12.20           O  
ANISOU  771  O   LEU A 112     1371   1681   1585   -215     24    -29       O  
ATOM    772  CB  LEU A 112      58.935  56.456  44.561  1.00 14.80           C  
ANISOU  772  CB  LEU A 112     1646   2059   1920   -190     39    -34       C  
ATOM    773  CG  LEU A 112      58.590  56.284  46.022  1.00 16.10           C  
ANISOU  773  CG  LEU A 112     1813   2213   2090   -186     25    -39       C  
ATOM    774  CD1 LEU A 112      57.644  55.112  46.103  1.00 16.17           C  
ANISOU  774  CD1 LEU A 112     1829   2214   2100   -161     25    -47       C  
ATOM    775  CD2 LEU A 112      59.846  56.012  46.866  1.00 18.55           C  
ANISOU  775  CD2 LEU A 112     2099   2543   2406   -191     21    -37       C  
ATOM    776  N   GLU A 113      58.823  59.433  43.778  1.00 12.87           N  
ANISOU  776  N   GLU A 113     1429   1795   1667   -237     38    -18       N  
ATOM    777  CA  GLU A 113      58.911  60.807  44.204  1.00 12.60           C  
ANISOU  777  CA  GLU A 113     1406   1748   1634   -261     32    -13       C  
ATOM    778  C   GLU A 113      57.748  61.656  43.693  1.00 12.34           C  
ANISOU  778  C   GLU A 113     1401   1691   1596   -262     32     -9       C  
ATOM    779  O   GLU A 113      57.267  62.532  44.400  1.00 13.51           O  
ANISOU  779  O   GLU A 113     1566   1820   1747   -271     23    -10       O  
ATOM    780  CB  GLU A 113      60.271  61.401  43.799  1.00 13.18           C  
ANISOU  780  CB  GLU A 113     1462   1839   1708   -284     38     -4       C  
ATOM    781  CG  GLU A 113      60.422  62.858  44.159  1.00 14.18           C  
ANISOU  781  CG  GLU A 113     1601   1951   1836   -311     32      2       C  
ATOM    782  CD  GLU A 113      60.661  63.121  45.615  1.00 14.26           C  
ANISOU  782  CD  GLU A 113     1610   1956   1853   -320     17     -5       C  
ATOM    783  OE1 GLU A 113      60.872  62.192  46.463  1.00 13.76           O  
ANISOU  783  OE1 GLU A 113     1532   1903   1792   -307     11    -12       O  
ATOM    784  OE2 GLU A 113      60.671  64.360  45.904  1.00 15.73           O  
ANISOU  784  OE2 GLU A 113     1811   2126   2041   -342     12     -2       O  
ATOM    785  N   ALA A 114      57.275  61.362  42.498  1.00 12.09           N  
ANISOU  785  N   ALA A 114     1375   1663   1558   -252     42     -6       N  
ATOM    786  CA  ALA A 114      56.185  62.068  41.874  1.00 11.84           C  
ANISOU  786  CA  ALA A 114     1366   1612   1520   -251     42     -2       C  
ATOM    787  C   ALA A 114      54.844  61.595  42.406  1.00 11.27           C  
ANISOU  787  C   ALA A 114     1309   1524   1449   -231     35    -10       C  
ATOM    788  O   ALA A 114      53.857  62.292  42.273  1.00 12.69           O  
ANISOU  788  O   ALA A 114     1510   1686   1627   -230     32     -6       O  
ATOM    789  CB  ALA A 114      56.209  61.875  40.361  1.00 12.26           C  
ANISOU  789  CB  ALA A 114     1417   1677   1562   -247     55      5       C  
ATOM    790  N   MET A 115      54.799  60.411  42.996  1.00 11.03           N  
ANISOU  790  N   MET A 115     1267   1501   1422   -215     31    -19       N  
ATOM    791  CA  MET A 115      53.489  59.810  43.397  1.00 10.55           C  
ANISOU  791  CA  MET A 115     1219   1427   1362   -195     25    -27       C  
ATOM    792  C   MET A 115      52.992  60.510  44.671  1.00 10.52           C  
ANISOU  792  C   MET A 115     1229   1405   1364   -199     14    -29       C  
ATOM    793  O   MET A 115      53.568  60.377  45.724  1.00 10.17           O  
ANISOU  793  O   MET A 115     1176   1364   1326   -203      8    -33       O  
ATOM    794  CB  MET A 115      53.624  58.300  43.615  1.00 10.36           C  
ANISOU  794  CB  MET A 115     1179   1415   1340   -177     26    -36       C  
ATOM    795  CG  MET A 115      52.304  57.696  44.073  1.00 10.26           C  
ANISOU  795  CG  MET A 115     1178   1389   1330   -160     20    -42       C  
ATOM    796  SD  MET A 115      52.322  55.893  44.163  1.00 10.77           S  
ANISOU  796  SD  MET A 115     1228   1465   1398   -138     23    -52       S  
ATOM    797  CE  MET A 115      53.415  55.542  45.541  1.00 10.94           C  
ANISOU  797  CE  MET A 115     1233   1496   1430   -141     17    -55       C  
ATOM    798  N   ARG A 116      51.882  61.263  44.520  1.00 10.36           N  
ANISOU  798  N   ARG A 116     1230   1366   1341   -197     11    -26       N  
ATOM    799  CA  ARG A 116      51.141  61.874  45.610  1.00 10.93           C  
ANISOU  799  CA  ARG A 116     1318   1418   1417   -197      2    -28       C  
ATOM    800  C   ARG A 116      49.740  61.276  45.808  1.00 10.63           C  
ANISOU  800  C   ARG A 116     1290   1371   1379   -175     -1    -33       C  
ATOM    801  O   ARG A 116      49.132  61.440  46.891  1.00 10.96           O  
ANISOU  801  O   ARG A 116     1340   1399   1424   -170     -9    -37       O  
ATOM    802  CB  ARG A 116      50.972  63.379  45.287  1.00 11.68           C  
ANISOU  802  CB  ARG A 116     1431   1496   1510   -211      3    -19       C  
ATOM    803  CG  ARG A 116      52.289  64.101  45.098  1.00 12.71           C  
ANISOU  803  CG  ARG A 116     1554   1633   1641   -235      7    -14       C  
ATOM    804  CD  ARG A 116      53.244  63.933  46.290  1.00 13.12           C  
ANISOU  804  CD  ARG A 116     1594   1692   1700   -245      0    -21       C  
ATOM    805  NE  ARG A 116      52.620  64.349  47.527  1.00 14.68           N  
ANISOU  805  NE  ARG A 116     1805   1871   1900   -243    -10    -28       N  
ATOM    806  CZ  ARG A 116      53.032  64.011  48.739  1.00 16.26           C  
ANISOU  806  CZ  ARG A 116     1998   2076   2104   -245    -18    -36       C  
ATOM    807  NH1 ARG A 116      54.131  63.258  48.909  1.00 17.08           N  
ANISOU  807  NH1 ARG A 116     2077   2202   2209   -248    -19    -38       N  
ATOM    808  NH2 ARG A 116      52.373  64.466  49.799  1.00 18.39           N  
ANISOU  808  NH2 ARG A 116     2284   2329   2375   -242    -26    -42       N  
ATOM    809  N   ASP A 117      49.240  60.636  44.761  1.00 10.86           N  
ANISOU  809  N   ASP A 117     1317   1407   1403   -164      4    -31       N  
ATOM    810  CA  ASP A 117      47.850  60.167  44.653  1.00 10.94           C  
ANISOU  810  CA  ASP A 117     1336   1410   1412   -147      2    -33       C  
ATOM    811  C   ASP A 117      47.816  58.785  44.118  1.00 10.75           C  
ANISOU  811  C   ASP A 117     1299   1400   1386   -135      5    -39       C  
ATOM    812  O   ASP A 117      48.600  58.455  43.279  1.00 11.18           O  
ANISOU  812  O   ASP A 117     1343   1469   1437   -139     12    -38       O  
ATOM    813  CB  ASP A 117      47.073  61.099  43.692  1.00 11.94           C  
ANISOU  813  CB  ASP A 117     1478   1527   1531   -148      4    -23       C  
ATOM    814  CG  ASP A 117      47.327  62.546  43.973  1.00 12.15           C  
ANISOU  814  CG  ASP A 117     1518   1539   1559   -163      4    -16       C  
ATOM    815  OD1 ASP A 117      46.976  62.960  45.093  1.00 13.11           O  
ANISOU  815  OD1 ASP A 117     1649   1647   1687   -162     -3    -20       O  
ATOM    816  OD2 ASP A 117      47.917  63.222  43.140  1.00 13.56           O  
ANISOU  816  OD2 ASP A 117     1698   1720   1733   -175      9     -8       O  
ATOM    817  N   VAL A 118      46.843  57.982  44.578  1.00  9.98           N  
ANISOU  817  N   VAL A 118     1204   1298   1291   -120      1    -45       N  
ATOM    818  CA  VAL A 118      46.560  56.698  43.968  1.00  9.92           C  
ANISOU  818  CA  VAL A 118     1187   1300   1281   -108      4    -51       C  
ATOM    819  C   VAL A 118      45.119  56.736  43.563  1.00  9.32           C  
ANISOU  819  C   VAL A 118     1123   1216   1201    -99      1    -49       C  
ATOM    820  O   VAL A 118      44.248  57.018  44.395  1.00 10.07           O  
ANISOU  820  O   VAL A 118     1227   1299   1301    -93     -5    -48       O  
ATOM    821  CB  VAL A 118      46.848  55.512  44.932  1.00 10.95           C  
ANISOU  821  CB  VAL A 118     1306   1434   1420    -99      2    -60       C  
ATOM    822  CG1 VAL A 118      46.581  54.179  44.290  1.00 11.34           C  
ANISOU  822  CG1 VAL A 118     1349   1491   1469    -87      6    -66       C  
ATOM    823  CG2 VAL A 118      48.290  55.615  45.411  1.00 12.09           C  
ANISOU  823  CG2 VAL A 118     1437   1587   1568   -108      3    -60       C  
ATOM    824  N   TYR A 119      44.827  56.412  42.317  1.00  8.72           N  
ANISOU  824  N   TYR A 119     1048   1149   1118    -96      5    -49       N  
ATOM    825  CA  TYR A 119      43.468  56.385  41.797  1.00  8.24           C  
ANISOU  825  CA  TYR A 119      996   1084   1052    -88      2    -46       C  
ATOM    826  C   TYR A 119      43.099  54.915  41.642  1.00  8.25           C  
ANISOU  826  C   TYR A 119      989   1091   1054    -78      2    -57       C  
ATOM    827  O   TYR A 119      43.706  54.198  40.836  1.00  8.82           O  
ANISOU  827  O   TYR A 119     1053   1176   1121    -79      8    -62       O  
ATOM    828  CB  TYR A 119      43.359  57.095  40.459  1.00  8.49           C  
ANISOU  828  CB  TYR A 119     1033   1121   1071    -94      6    -38       C  
ATOM    829  CG  TYR A 119      43.696  58.547  40.523  1.00  8.54           C  
ANISOU  829  CG  TYR A 119     1050   1120   1077   -104      7    -26       C  
ATOM    830  CD1 TYR A 119      42.698  59.506  40.818  1.00  8.75           C  
ANISOU  830  CD1 TYR A 119     1089   1131   1103   -101      2    -18       C  
ATOM    831  CD2 TYR A 119      44.998  59.022  40.240  1.00  9.14           C  
ANISOU  831  CD2 TYR A 119     1120   1201   1151   -117     13    -23       C  
ATOM    832  CE1 TYR A 119      42.990  60.841  40.855  1.00  8.91           C  
ANISOU  832  CE1 TYR A 119     1120   1141   1123   -110      3     -8       C  
ATOM    833  CE2 TYR A 119      45.273  60.394  40.261  1.00  9.52           C  
ANISOU  833  CE2 TYR A 119     1179   1240   1199   -129     14    -12       C  
ATOM    834  CZ  TYR A 119      44.283  61.299  40.552  1.00  9.40           C  
ANISOU  834  CZ  TYR A 119     1179   1208   1185   -125      9     -5       C  
ATOM    835  OH  TYR A 119      44.557  62.658  40.551  1.00 10.21           O  
ANISOU  835  OH  TYR A 119     1294   1299   1288   -136     11      6       O  
ATOM    836  N   ILE A 120      42.032  54.500  42.323  1.00  8.00           N  
ANISOU  836  N   ILE A 120      959   1051   1027    -69     -5    -59       N  
ATOM    837  CA  ILE A 120      41.628  53.073  42.297  1.00  8.43           C  
ANISOU  837  CA  ILE A 120     1008   1110   1085    -60     -5    -70       C  
ATOM    838  C   ILE A 120      40.307  52.991  41.570  1.00  8.28           C  
ANISOU  838  C   ILE A 120      995   1092   1060    -56     -9    -68       C  
ATOM    839  O   ILE A 120      39.324  53.643  41.979  1.00  8.34           O  
ANISOU  839  O   ILE A 120     1010   1091   1068    -53    -15    -61       O  
ATOM    840  CB  ILE A 120      41.524  52.536  43.752  1.00  9.05           C  
ANISOU  840  CB  ILE A 120     1083   1180   1176    -54     -9    -73       C  
ATOM    841  CG1 ILE A 120      42.891  52.689  44.466  1.00  9.23           C  
ANISOU  841  CG1 ILE A 120     1099   1205   1204    -59     -6    -74       C  
ATOM    842  CG2 ILE A 120      41.036  51.101  43.735  1.00  8.99           C  
ANISOU  842  CG2 ILE A 120     1070   1173   1172    -46     -9    -82       C  
ATOM    843  CD1 ILE A 120      42.883  52.339  45.939  1.00 10.01           C  
ANISOU  843  CD1 ILE A 120     1195   1296   1313    -54    -10    -75       C  
ATOM    844  N   VAL A 121      40.292  52.230  40.486  1.00  8.06           N  
ANISOU  844  N   VAL A 121      964   1074   1024    -56     -6    -74       N  
ATOM    845  CA  VAL A 121      39.144  52.126  39.599  1.00  8.08           C  
ANISOU  845  CA  VAL A 121      972   1082   1018    -54    -10    -74       C  
ATOM    846  C   VAL A 121      38.398  50.852  39.976  1.00  8.11           C  
ANISOU  846  C   VAL A 121      971   1081   1028    -48    -14    -83       C  
ATOM    847  O   VAL A 121      39.037  49.757  40.114  1.00  8.09           O  
ANISOU  847  O   VAL A 121      963   1081   1032    -47    -10    -94       O  
ATOM    848  CB  VAL A 121      39.611  52.076  38.105  1.00  8.27           C  
ANISOU  848  CB  VAL A 121      995   1119   1027    -60     -5    -76       C  
ATOM    849  CG1 VAL A 121      38.391  51.986  37.152  1.00  8.29           C  
ANISOU  849  CG1 VAL A 121     1003   1129   1018    -58    -11    -75       C  
ATOM    850  CG2 VAL A 121      40.509  53.265  37.786  1.00  8.75           C  
ANISOU  850  CG2 VAL A 121     1059   1183   1082    -67      1    -65       C  
ATOM    851  N   GLN A 122      37.074  50.944  40.138  1.00  8.38           N  
ANISOU  851  N   GLN A 122     1009   1113   1064    -44    -22    -79       N  
ATOM    852  CA  GLN A 122      36.242  49.853  40.592  1.00  8.34           C  
ANISOU  852  CA  GLN A 122      999   1103   1065    -40    -26    -86       C  
ATOM    853  C   GLN A 122      34.916  49.865  39.818  1.00  8.50           C  
ANISOU  853  C   GLN A 122     1021   1131   1078    -40    -33    -84       C  
ATOM    854  O   GLN A 122      34.522  50.894  39.211  1.00  9.14           O  
ANISOU  854  O   GLN A 122     1108   1217   1149    -41    -36    -74       O  
ATOM    855  CB  GLN A 122      36.004  49.988  42.112  1.00  8.21           C  
ANISOU  855  CB  GLN A 122      982   1076   1063    -34    -28    -82       C  
ATOM    856  CG  GLN A 122      37.319  50.005  42.907  1.00  8.24           C  
ANISOU  856  CG  GLN A 122      982   1074   1073    -35    -23    -84       C  
ATOM    857  CD  GLN A 122      37.101  50.099  44.410  1.00  8.42           C  
ANISOU  857  CD  GLN A 122     1005   1087   1108    -29    -25    -81       C  
ATOM    858  OE1 GLN A 122      36.909  51.189  44.942  1.00  8.34           O  
ANISOU  858  OE1 GLN A 122     1000   1072   1097    -29    -28    -72       O  
ATOM    859  NE2 GLN A 122      37.198  48.975  45.090  1.00  9.11           N  
ANISOU  859  NE2 GLN A 122     1087   1171   1204    -25    -25    -87       N  
ATOM    860  N   ASP A 123      34.199  48.757  39.874  1.00  9.11           N  
ANISOU  860  N   ASP A 123     1095   1208   1159    -39    -37    -92       N  
ATOM    861  CA  ASP A 123      32.879  48.690  39.254  1.00  9.67           C  
ANISOU  861  CA  ASP A 123     1166   1286   1224    -41    -45    -90       C  
ATOM    862  C   ASP A 123      31.993  49.799  39.790  1.00  9.88           C  
ANISOU  862  C   ASP A 123     1192   1309   1251    -35    -50    -74       C  
ATOM    863  O   ASP A 123      31.944  50.018  41.018  1.00  9.15           O  
ANISOU  863  O   ASP A 123     1100   1206   1170    -30    -49    -70       O  
ATOM    864  CB  ASP A 123      32.226  47.310  39.512  1.00 10.88           C  
ANISOU  864  CB  ASP A 123     1313   1435   1384    -42    -48   -101       C  
ATOM    865  CG  ASP A 123      32.905  46.180  38.811  1.00 11.85           C  
ANISOU  865  CG  ASP A 123     1437   1561   1505    -47    -43   -117       C  
ATOM    866  OD1 ASP A 123      33.616  46.379  37.790  1.00 13.79           O  
ANISOU  866  OD1 ASP A 123     1686   1816   1738    -50    -39   -121       O  
ATOM    867  OD2 ASP A 123      32.683  45.029  39.332  1.00 14.06           O  
ANISOU  867  OD2 ASP A 123     1714   1832   1796    -47    -43   -126       O  
ATOM    868  N   LEU A 124      31.227  50.435  38.913  1.00  9.55           N  
ANISOU  868  N   LEU A 124     1153   1279   1198    -36    -55    -66       N  
ATOM    869  CA  LEU A 124      30.233  51.435  39.295  1.00 10.25           C  
ANISOU  869  CA  LEU A 124     1242   1366   1287    -29    -61    -51       C  
ATOM    870  C   LEU A 124      28.956  50.777  39.762  1.00 10.95           C  
ANISOU  870  C   LEU A 124     1324   1456   1383    -26    -67    -51       C  
ATOM    871  O   LEU A 124      28.404  49.927  39.036  1.00 13.03           O  
ANISOU  871  O   LEU A 124     1582   1729   1641    -32    -73    -59       O  
ATOM    872  CB  LEU A 124      29.996  52.405  38.128  1.00 10.33           C  
ANISOU  872  CB  LEU A 124     1257   1387   1282    -29    -63    -41       C  
ATOM    873  CG  LEU A 124      29.086  53.590  38.413  1.00 10.53           C  
ANISOU  873  CG  LEU A 124     1284   1409   1306    -20    -67    -23       C  
ATOM    874  CD1 LEU A 124      29.648  54.463  39.515  1.00 10.68           C  
ANISOU  874  CD1 LEU A 124     1310   1412   1335    -15    -61    -18       C  
ATOM    875  CD2 LEU A 124      28.857  54.360  37.150  1.00 11.74           C  
ANISOU  875  CD2 LEU A 124     1441   1575   1443    -21    -70    -13       C  
ATOM    876  N   MET A 125      28.489  51.120  40.954  1.00 10.43           N  
ANISOU  876  N   MET A 125     1255   1379   1327    -18    -67    -44       N  
ATOM    877  CA  MET A 125      27.223  50.647  41.488  1.00 10.37           C  
ANISOU  877  CA  MET A 125     1240   1374   1327    -14    -73    -41       C  
ATOM    878  C   MET A 125      26.245  51.807  41.525  1.00 10.56           C  
ANISOU  878  C   MET A 125     1264   1401   1348     -5    -76    -25       C  
ATOM    879  O   MET A 125      26.552  52.917  41.064  1.00 11.30           O  
ANISOU  879  O   MET A 125     1365   1495   1433     -2    -75    -16       O  
ATOM    880  CB  MET A 125      27.455  50.028  42.879  1.00 10.47           C  
ANISOU  880  CB  MET A 125     1250   1373   1354    -11    -68    -46       C  
ATOM    881  CG  MET A 125      28.494  48.920  42.849  1.00 11.41           C  
ANISOU  881  CG  MET A 125     1370   1488   1478    -19    -64    -61       C  
ATOM    882  SD  MET A 125      27.984  47.424  42.109  1.00 12.48           S  
ANISOU  882  SD  MET A 125     1498   1630   1612    -28    -68    -73       S  
ATOM    883  CE  MET A 125      27.038  46.745  43.454  1.00 13.19           C  
ANISOU  883  CE  MET A 125     1580   1712   1718    -24    -70    -70       C  
ATOM    884  N   GLU A 126      25.012  51.539  41.933  1.00 11.06           N  
ANISOU  884  N   GLU A 126     1318   1469   1415     -1    -81    -20       N  
ATOM    885  CA  GLU A 126      23.962  52.558  41.830  1.00 11.86           C  
ANISOU  885  CA  GLU A 126     1417   1576   1513     10    -85     -3       C  
ATOM    886  C   GLU A 126      23.819  53.343  43.130  1.00 10.87           C  
ANISOU  886  C   GLU A 126     1296   1438   1397     23    -80      5       C  
ATOM    887  O   GLU A 126      23.532  54.523  43.135  1.00 10.70           O  
ANISOU  887  O   GLU A 126     1280   1414   1372     33    -78     17       O  
ATOM    888  CB  GLU A 126      22.667  51.839  41.539  1.00 13.96           C  
ANISOU  888  CB  GLU A 126     1669   1857   1779      7    -94     -2       C  
ATOM    889  CG  GLU A 126      21.440  52.711  41.463  1.00 18.25           C  
ANISOU  889  CG  GLU A 126     2206   2409   2319     19    -98     16       C  
ATOM    890  CD  GLU A 126      21.398  53.560  40.218  1.00 23.69           C  
ANISOU  890  CD  GLU A 126     2899   3109   2993     20   -103     24       C  
ATOM    891  OE1 GLU A 126      22.227  53.356  39.308  1.00 27.75           O  
ANISOU  891  OE1 GLU A 126     3420   3627   3498     10   -103     16       O  
ATOM    892  OE2 GLU A 126      20.511  54.449  40.169  1.00 33.34           O  
ANISOU  892  OE2 GLU A 126     4118   4337   4213     32   -105     41       O  
ATOM    893  N   THR A 127      23.980  52.670  44.242  1.00  9.69           N  
ANISOU  893  N   THR A 127     1143   1279   1258     23    -76     -2       N  
ATOM    894  CA  THR A 127      23.743  53.273  45.514  1.00  9.73           C  
ANISOU  894  CA  THR A 127     1152   1273   1271     34    -71      5       C  
ATOM    895  C   THR A 127      24.481  52.504  46.599  1.00  9.33           C  
ANISOU  895  C   THR A 127     1102   1212   1230     31    -66     -5       C  
ATOM    896  O   THR A 127      25.252  51.571  46.294  1.00  8.85           O  
ANISOU  896  O   THR A 127     1040   1151   1171     21    -66    -17       O  
ATOM    897  CB  THR A 127      22.216  53.358  45.800  1.00 10.00           C  
ANISOU  897  CB  THR A 127     1175   1316   1308     44    -74     16       C  
ATOM    898  OG1 THR A 127      21.984  54.238  46.905  1.00 10.94           O  
ANISOU  898  OG1 THR A 127     1300   1426   1432     58    -68     24       O  
ATOM    899  CG2 THR A 127      21.610  51.976  46.077  1.00  9.92           C  
ANISOU  899  CG2 THR A 127     1151   1313   1306     37    -77     10       C  
ATOM    900  N   ASP A 128      24.200  52.870  47.848  1.00  9.24           N  
ANISOU  900  N   ASP A 128     1093   1193   1226     41    -61     -1       N  
ATOM    901  CA  ASP A 128      24.630  52.044  48.978  1.00  9.04           C  
ANISOU  901  CA  ASP A 128     1066   1161   1210     40    -57     -8       C  
ATOM    902  C   ASP A 128      23.511  51.866  49.963  1.00  8.60           C  
ANISOU  902  C   ASP A 128     1003   1106   1160     49    -56     -1       C  
ATOM    903  O   ASP A 128      22.451  52.473  49.830  1.00  9.33           O  
ANISOU  903  O   ASP A 128     1091   1205   1251     58    -57     10       O  
ATOM    904  CB  ASP A 128      25.929  52.596  49.580  1.00  9.49           C  
ANISOU  904  CB  ASP A 128     1135   1205   1266     40    -52    -13       C  
ATOM    905  CG  ASP A 128      25.768  53.952  50.216  1.00 10.27           C  
ANISOU  905  CG  ASP A 128     1243   1296   1362     51    -49     -5       C  
ATOM    906  OD1 ASP A 128      24.833  54.093  51.015  1.00 11.02           O  
ANISOU  906  OD1 ASP A 128     1336   1391   1461     61    -47      1       O  
ATOM    907  OD2 ASP A 128      26.579  54.878  49.931  1.00 11.91           O  
ANISOU  907  OD2 ASP A 128     1462   1497   1565     49    -47     -6       O  
ATOM    908  N   LEU A 129      23.676  50.932  50.886  1.00  8.09           N  
ANISOU  908  N   LEU A 129      933   1037   1102     47    -53     -6       N  
ATOM    909  CA  LEU A 129      22.553  50.613  51.765  1.00  8.43           C  
ANISOU  909  CA  LEU A 129      967   1084   1152     54    -51      2       C  
ATOM    910  C   LEU A 129      22.203  51.759  52.709  1.00  8.54           C  
ANISOU  910  C   LEU A 129      987   1092   1164     70    -46     10       C  
ATOM    911  O   LEU A 129      21.052  51.865  53.161  1.00  9.48           O  
ANISOU  911  O   LEU A 129     1099   1218   1286     79    -44     19       O  
ATOM    912  CB  LEU A 129      22.855  49.376  52.595  1.00  8.27           C  
ANISOU  912  CB  LEU A 129      942   1059   1140     49    -49     -4       C  
ATOM    913  CG  LEU A 129      21.659  48.820  53.437  1.00  8.65           C  
ANISOU  913  CG  LEU A 129      979   1112   1195     54    -47      4       C  
ATOM    914  CD1 LEU A 129      20.497  48.335  52.597  1.00  9.00           C  
ANISOU  914  CD1 LEU A 129     1009   1169   1241     48    -53      9       C  
ATOM    915  CD2 LEU A 129      22.135  47.682  54.326  1.00  8.72           C  
ANISOU  915  CD2 LEU A 129      986   1114   1212     49    -43      0       C  
ATOM    916  N   TYR A 130      23.161  52.605  53.048  1.00  8.88           N  
ANISOU  916  N   TYR A 130     1045   1126   1204     72    -43      7       N  
ATOM    917  CA  TYR A 130      22.837  53.794  53.855  1.00  9.66           C  
ANISOU  917  CA  TYR A 130     1153   1219   1300     87    -37     13       C  
ATOM    918  C   TYR A 130      21.844  54.675  53.120  1.00  9.89           C  
ANISOU  918  C   TYR A 130     1180   1253   1325     96    -39     24       C  
ATOM    919  O   TYR A 130      20.800  55.064  53.651  1.00  9.67           O  
ANISOU  919  O   TYR A 130     1148   1228   1298    109    -35     33       O  
ATOM    920  CB  TYR A 130      24.110  54.566  54.192  1.00  9.92           C  
ANISOU  920  CB  TYR A 130     1202   1238   1329     85    -35      6       C  
ATOM    921  CG  TYR A 130      23.887  55.852  54.939  1.00 10.79           C  
ANISOU  921  CG  TYR A 130     1325   1340   1436     98    -29     10       C  
ATOM    922  CD1 TYR A 130      23.835  55.858  56.299  1.00 10.85           C  
ANISOU  922  CD1 TYR A 130     1335   1342   1444    105    -24      9       C  
ATOM    923  CD2 TYR A 130      23.694  57.038  54.280  1.00 11.33           C  
ANISOU  923  CD2 TYR A 130     1402   1404   1500    103    -29     16       C  
ATOM    924  CE1 TYR A 130      23.639  57.024  57.011  1.00 12.24           C  
ANISOU  924  CE1 TYR A 130     1525   1510   1616    117    -18     11       C  
ATOM    925  CE2 TYR A 130      23.461  58.193  54.973  1.00 12.03           C  
ANISOU  925  CE2 TYR A 130     1503   1482   1585    116    -23     19       C  
ATOM    926  CZ  TYR A 130      23.360  58.150  56.320  1.00 12.69           C  
ANISOU  926  CZ  TYR A 130     1591   1562   1671    124    -18     16       C  
ATOM    927  OH  TYR A 130      23.193  59.312  57.062  1.00 14.32           O  
ANISOU  927  OH  TYR A 130     1811   1756   1873    136    -11     17       O  
ATOM    928  N   LYS A 131      22.170  54.987  51.888  1.00  9.70           N  
ANISOU  928  N   LYS A 131     1159   1231   1296     89    -43     23       N  
ATOM    929  CA  LYS A 131      21.288  55.842  51.053  1.00 10.27           C  
ANISOU  929  CA  LYS A 131     1229   1310   1363     98    -46     35       C  
ATOM    930  C   LYS A 131      19.941  55.154  50.876  1.00 10.08           C  
ANISOU  930  C   LYS A 131     1187   1302   1342    101    -50     43       C  
ATOM    931  O   LYS A 131      18.871  55.812  50.971  1.00 11.44           O  
ANISOU  931  O   LYS A 131     1354   1479   1514    115    -48     55       O  
ATOM    932  CB  LYS A 131      21.965  56.204  49.723  1.00 10.76           C  
ANISOU  932  CB  LYS A 131     1298   1373   1419     89    -50     33       C  
ATOM    933  CG  LYS A 131      23.241  57.029  49.938  1.00 12.03           C  
ANISOU  933  CG  LYS A 131     1476   1518   1577     86    -46     28       C  
ATOM    934  CD  LYS A 131      23.779  57.745  48.702  1.00 14.10           C  
ANISOU  934  CD  LYS A 131     1747   1780   1831     81    -49     31       C  
ATOM    935  CE  LYS A 131      24.420  56.832  47.770  1.00 13.83           C  
ANISOU  935  CE  LYS A 131     1706   1754   1793     65    -53     23       C  
ATOM    936  NZ  LYS A 131      25.100  57.531  46.583  1.00 13.90           N  
ANISOU  936  NZ  LYS A 131     1724   1763   1794     59    -55     25       N  
ATOM    937  N   LEU A 132      19.941  53.847  50.627  1.00 10.13           N  
ANISOU  937  N   LEU A 132     1181   1316   1352     87    -54     36       N  
ATOM    938  CA  LEU A 132      18.723  53.167  50.362  1.00 10.31           C  
ANISOU  938  CA  LEU A 132     1186   1353   1377     87    -59     42       C  
ATOM    939  C   LEU A 132      17.795  53.175  51.581  1.00 10.08           C  
ANISOU  939  C   LEU A 132     1150   1326   1355     99    -52     51       C  
ATOM    940  O   LEU A 132      16.574  53.395  51.453  1.00 10.58           O  
ANISOU  940  O   LEU A 132     1200   1401   1417    108    -54     62       O  
ATOM    941  CB  LEU A 132      18.990  51.763  49.859  1.00 11.12           C  
ANISOU  941  CB  LEU A 132     1281   1461   1483     68    -64     32       C  
ATOM    942  CG  LEU A 132      17.834  50.921  49.452  1.00 12.12           C  
ANISOU  942  CG  LEU A 132     1389   1603   1612     62    -71     36       C  
ATOM    943  CD1 LEU A 132      17.057  51.571  48.313  1.00 13.37           C  
ANISOU  943  CD1 LEU A 132     1541   1777   1763     65    -78     46       C  
ATOM    944  CD2 LEU A 132      18.359  49.553  49.052  1.00 12.83           C  
ANISOU  944  CD2 LEU A 132     1476   1692   1706     43    -75     23       C  
ATOM    945  N   LEU A 133      18.338  52.929  52.765  1.00  9.57           N  
ANISOU  945  N   LEU A 133     1091   1250   1294    101    -46     45       N  
ATOM    946  CA  LEU A 133      17.528  52.894  54.002  1.00  9.84           C  
ANISOU  946  CA  LEU A 133     1119   1286   1333    113    -38     52       C  
ATOM    947  C   LEU A 133      17.047  54.278  54.400  1.00 10.83           C  
ANISOU  947  C   LEU A 133     1252   1409   1455    133    -32     61       C  
ATOM    948  O   LEU A 133      16.025  54.387  55.102  1.00 11.58           O  
ANISOU  948  O   LEU A 133     1338   1510   1552    146    -27     71       O  
ATOM    949  CB  LEU A 133      18.289  52.252  55.138  1.00 10.10           C  
ANISOU  949  CB  LEU A 133     1158   1309   1370    109    -33     44       C  
ATOM    950  CG  LEU A 133      18.492  50.781  54.909  1.00  9.68           C  
ANISOU  950  CG  LEU A 133     1095   1260   1324     92    -37     38       C  
ATOM    951  CD1 LEU A 133      19.322  50.249  56.097  1.00 10.56           C  
ANISOU  951  CD1 LEU A 133     1214   1361   1439     91    -32     32       C  
ATOM    952  CD2 LEU A 133      17.203  49.997  54.775  1.00 10.92           C  
ANISOU  952  CD2 LEU A 133     1233   1431   1487     89    -40     46       C  
ATOM    953  N   LYS A 134      17.707  55.365  53.987  1.00 10.71           N  
ANISOU  953  N   LYS A 134     1253   1383   1433    137    -32     59       N  
ATOM    954  CA  LYS A 134      17.100  56.680  54.197  1.00 11.86           C  
ANISOU  954  CA  LYS A 134     1406   1526   1576    157    -26     69       C  
ATOM    955  C   LYS A 134      15.914  56.905  53.291  1.00 12.85           C  
ANISOU  955  C   LYS A 134     1516   1666   1700    164    -31     83       C  
ATOM    956  O   LYS A 134      14.972  57.636  53.696  1.00 14.31           O  
ANISOU  956  O   LYS A 134     1698   1854   1885    183    -25     94       O  
ATOM    957  CB  LYS A 134      18.107  57.787  54.004  1.00 11.09           C  
ANISOU  957  CB  LYS A 134     1330   1411   1473    158    -24     64       C  
ATOM    958  CG  LYS A 134      19.240  57.769  55.022  1.00 12.04           C  
ANISOU  958  CG  LYS A 134     1465   1516   1593    153    -19     52       C  
ATOM    959  CD  LYS A 134      18.747  58.029  56.404  1.00 13.27           C  
ANISOU  959  CD  LYS A 134     1624   1669   1750    168    -10     53       C  
ATOM    960  CE  LYS A 134      19.906  58.112  57.412  1.00 14.81           C  
ANISOU  960  CE  LYS A 134     1834   1850   1943    163     -6     41       C  
ATOM    961  NZ  LYS A 134      19.388  58.419  58.781  1.00 17.58           N  
ANISOU  961  NZ  LYS A 134     2189   2197   2292    178      3     42       N  
ATOM    962  N   SER A 135      15.927  56.254  52.140  1.00 13.50           N  
ANISOU  962  N   SER A 135     1589   1760   1781    149    -41     82       N  
ATOM    963  CA ASER A 135      14.945  56.521  51.067  0.50 14.66           C  
ANISOU  963  CA ASER A 135     1723   1924   1925    154    -48     94       C  
ATOM    964  CA BSER A 135      14.945  56.543  51.073  0.50 14.69           C  
ANISOU  964  CA BSER A 135     1726   1926   1927    154    -48     95       C  
ATOM    965  C   SER A 135      13.699  55.688  51.190  1.00 15.68           C  
ANISOU  965  C   SER A 135     1828   2072   2059    153    -51    102       C  
ATOM    966  O   SER A 135      12.635  56.082  50.746  1.00 19.04           O  
ANISOU  966  O   SER A 135     2240   2511   2482    164    -53    116       O  
ATOM    967  CB ASER A 135      15.549  56.222  49.704  0.50 14.91           C  
ANISOU  967  CB ASER A 135     1755   1959   1950    137    -58     89       C  
ATOM    968  CB BSER A 135      15.577  56.397  49.666  0.50 15.08           C  
ANISOU  968  CB BSER A 135     1780   1980   1971    139    -57     90       C  
ATOM    969  OG ASER A 135      14.583  56.446  48.691  0.50 16.38           O  
ANISOU  969  OG ASER A 135     1929   2163   2131    141    -66    101       O  
ATOM    970  OG BSER A 135      15.788  55.057  49.267  0.50 15.93           O  
ANISOU  970  OG BSER A 135     1877   2095   2080    119    -64     80       O  
ATOM    971  N   GLN A 136      13.792  54.493  51.709  1.00 15.11           N  
ANISOU  971  N   GLN A 136     1748   2000   1992    140    -51     94       N  
ATOM    972  CA  GLN A 136      12.590  53.656  51.739  1.00 15.86           C  
ANISOU  972  CA  GLN A 136     1819   2115   2093    137    -54    102       C  
ATOM    973  C   GLN A 136      12.665  52.511  52.705  1.00 14.40           C  
ANISOU  973  C   GLN A 136     1628   1927   1916    127    -50     96       C  
ATOM    974  O   GLN A 136      13.742  52.030  53.072  1.00 13.53           O  
ANISOU  974  O   GLN A 136     1530   1802   1807    118    -48     83       O  
ATOM    975  CB  GLN A 136      12.295  53.089  50.359  1.00 18.57           C  
ANISOU  975  CB  GLN A 136     2150   2473   2432    121    -68    102       C  
ATOM    976  CG  GLN A 136      13.333  52.075  49.941  1.00 20.33           C  
ANISOU  976  CG  GLN A 136     2380   2689   2656     99    -73     85       C  
ATOM    977  CD  GLN A 136      12.998  51.373  48.623  1.00 25.91           C  
ANISOU  977  CD  GLN A 136     3074   3411   3358     82    -86     82       C  
ATOM    978  OE1 GLN A 136      13.366  51.849  47.570  1.00 28.46           O  
ANISOU  978  OE1 GLN A 136     3405   3737   3673     80    -92     81       O  
ATOM    979  NE2 GLN A 136      12.339  50.195  48.700  1.00 28.82           N  
ANISOU  979  NE2 GLN A 136     3427   3791   3734     68    -90     81       N  
ATOM    980  N   GLN A 137      11.499  52.039  53.087  1.00 13.73           N  
ANISOU  980  N   GLN A 137     1523   1856   1836    130    -49    106       N  
ATOM    981  CA  GLN A 137      11.337  50.832  53.810  1.00 14.54           C  
ANISOU  981  CA  GLN A 137     1617   1961   1948    118    -47    103       C  
ATOM    982  C   GLN A 137      11.533  49.690  52.834  1.00 14.16           C  
ANISOU  982  C   GLN A 137     1562   1917   1902     94    -58     94       C  
ATOM    983  O   GLN A 137      11.095  49.746  51.687  1.00 16.42           O  
ANISOU  983  O   GLN A 137     1840   2217   2184     88    -68     96       O  
ATOM    984  CB  GLN A 137       9.932  50.776  54.363  1.00 15.84           C  
ANISOU  984  CB  GLN A 137     1760   2143   2117    128    -42    118       C  
ATOM    985  CG  GLN A 137       9.679  49.592  55.196  1.00 18.15           C  
ANISOU  985  CG  GLN A 137     2043   2436   2419    117    -38    118       C  
ATOM    986  CD  GLN A 137       8.385  49.750  55.919  1.00 22.85           C  
ANISOU  986  CD  GLN A 137     2618   3046   3016    131    -31    134       C  
ATOM    987  OE1 GLN A 137       7.366  50.062  55.302  1.00 26.39           O  
ANISOU  987  OE1 GLN A 137     3050   3514   3465    135    -36    146       O  
ATOM    988  NE2 GLN A 137       8.451  49.688  57.274  1.00 22.61           N  
ANISOU  988  NE2 GLN A 137     2592   3009   2989    140    -18    136       N  
ATOM    989  N   LEU A 138      12.284  48.707  53.249  1.00 13.27           N  
ANISOU  989  N   LEU A 138     1455   1792   1794     80    -57     83       N  
ATOM    990  CA  LEU A 138      12.498  47.491  52.434  1.00 13.20           C  
ANISOU  990  CA  LEU A 138     1441   1785   1789     57    -66     73       C  
ATOM    991  C   LEU A 138      11.472  46.450  52.729  1.00 13.36           C  
ANISOU  991  C   LEU A 138     1442   1816   1818     46    -67     79       C  
ATOM    992  O   LEU A 138      11.087  46.251  53.887  1.00 14.44           O  
ANISOU  992  O   LEU A 138     1574   1952   1962     53    -58     86       O  
ATOM    993  CB  LEU A 138      13.884  46.887  52.769  1.00 13.15           C  
ANISOU  993  CB  LEU A 138     1452   1758   1785     49    -62     58       C  
ATOM    994  CG  LEU A 138      15.053  47.778  52.368  1.00 13.41           C  
ANISOU  994  CG  LEU A 138     1505   1781   1809     55    -62     50       C  
ATOM    995  CD1 LEU A 138      16.311  47.027  52.782  1.00 13.02           C  
ANISOU  995  CD1 LEU A 138     1468   1715   1764     46    -59     37       C  
ATOM    996  CD2 LEU A 138      15.028  48.200  50.889  1.00 14.28           C  
ANISOU  996  CD2 LEU A 138     1616   1901   1911     49    -72     48       C  
ATOM    997  N   SER A 139      11.135  45.681  51.688  1.00 13.04           N  
ANISOU  997  N   SER A 139     1392   1785   1778     27    -78     74       N  
ATOM    998  CA  SER A 139      10.294  44.509  51.899  1.00 13.48           C  
ANISOU  998  CA  SER A 139     1429   1847   1843     11    -80     77       C  
ATOM    999  C   SER A 139      11.086  43.473  52.669  1.00 12.96           C  
ANISOU  999  C   SER A 139     1373   1762   1787      2    -74     67       C  
ATOM   1000  O   SER A 139      12.322  43.442  52.608  1.00 12.49           O  
ANISOU 1000  O   SER A 139     1333   1687   1725      2    -72     55       O  
ATOM   1001  CB  SER A 139       9.842  43.889  50.557  1.00 14.90           C  
ANISOU 1001  CB  SER A 139     1599   2040   2021     -9    -95     71       C  
ATOM   1002  OG  SER A 139      10.917  43.342  49.880  1.00 15.63           O  
ANISOU 1002  OG  SER A 139     1708   2120   2112    -22    -99     53       O  
ATOM   1003  N   ASN A 140      10.393  42.517  53.261  1.00 12.58           N  
ANISOU 1003  N   ASN A 140     1313   1718   1751     -8    -71     73       N  
ATOM   1004  CA  ASN A 140      11.057  41.329  53.874  1.00 12.28           C  
ANISOU 1004  CA  ASN A 140     1283   1661   1722    -19    -66     65       C  
ATOM   1005  C   ASN A 140      11.903  40.593  52.838  1.00 12.57           C  
ANISOU 1005  C   ASN A 140     1331   1686   1758    -37    -74     47       C  
ATOM   1006  O   ASN A 140      12.988  40.094  53.192  1.00 12.17           O  
ANISOU 1006  O   ASN A 140     1296   1617   1712    -38    -69     37       O  
ATOM   1007  CB  ASN A 140      10.023  40.373  54.475  1.00 13.07           C  
ANISOU 1007  CB  ASN A 140     1364   1766   1834    -31    -63     75       C  
ATOM   1008  CG  ASN A 140      10.642  39.255  55.242  1.00 13.00           C  
ANISOU 1008  CG  ASN A 140     1365   1739   1836    -39    -56     71       C  
ATOM   1009  OD1 ASN A 140      11.490  39.474  56.112  1.00 13.43           O  
ANISOU 1009  OD1 ASN A 140     1432   1780   1889    -26    -47     70       O  
ATOM   1010  ND2 ASN A 140      10.259  38.027  54.908  1.00 14.05           N  
ANISOU 1010  ND2 ASN A 140     1490   1869   1979    -62    -61     67       N  
ATOM   1011  N   ASP A 141      11.453  40.493  51.592  1.00 13.00           N  
ANISOU 1011  N   ASP A 141     1378   1753   1808    -50    -86     42       N  
ATOM   1012  CA  ASP A 141      12.231  39.808  50.537  1.00 13.00           C  
ANISOU 1012  CA  ASP A 141     1390   1743   1806    -66    -93     23       C  
ATOM   1013  C   ASP A 141      13.585  40.499  50.387  1.00 12.86           C  
ANISOU 1013  C   ASP A 141     1393   1714   1780    -54    -89     14       C  
ATOM   1014  O   ASP A 141      14.607  39.832  50.240  1.00 11.74           O  
ANISOU 1014  O   ASP A 141     1265   1556   1641    -60    -87      1       O  
ATOM   1015  CB  ASP A 141      11.529  39.854  49.139  1.00 14.49           C  
ANISOU 1015  CB  ASP A 141     1569   1951   1987    -80   -107     19       C  
ATOM   1016  CG  ASP A 141      10.189  39.091  49.041  1.00 17.67           C  
ANISOU 1016  CG  ASP A 141     1949   2367   2396    -97   -114     26       C  
ATOM   1017  OD1 ASP A 141       9.960  38.007  49.579  1.00 15.02           O  
ANISOU 1017  OD1 ASP A 141     1610   2023   2073   -110   -111     25       O  
ATOM   1018  OD2 ASP A 141       9.397  39.561  48.156  1.00 23.83           O  
ANISOU 1018  OD2 ASP A 141     2716   3169   3167   -100   -125     30       O  
ATOM   1019  N   HIS A 142      13.573  41.821  50.339  1.00 12.31           N  
ANISOU 1019  N   HIS A 142     1325   1653   1700    -37    -89     22       N  
ATOM   1020  CA  HIS A 142      14.815  42.555  50.075  1.00 12.79           C  
ANISOU 1020  CA  HIS A 142     1404   1704   1752    -27    -86     14       C  
ATOM   1021  C   HIS A 142      15.753  42.501  51.285  1.00 11.23           C  
ANISOU 1021  C   HIS A 142     1218   1489   1561    -17    -75     13       C  
ATOM   1022  O   HIS A 142      16.959  42.368  51.120  1.00 10.52           O  
ANISOU 1022  O   HIS A 142     1142   1386   1469    -18    -73      2       O  
ATOM   1023  CB  HIS A 142      14.557  43.984  49.673  1.00 14.77           C  
ANISOU 1023  CB  HIS A 142     1654   1966   1991    -12    -89     23       C  
ATOM   1024  CG  HIS A 142      14.029  44.098  48.281  1.00 19.72           C  
ANISOU 1024  CG  HIS A 142     2274   2610   2609    -21   -101     21       C  
ATOM   1025  ND1 HIS A 142      14.807  43.850  47.174  1.00 26.14           N  
ANISOU 1025  ND1 HIS A 142     3097   3420   3415    -32   -107      7       N  
ATOM   1026  CD2 HIS A 142      12.782  44.315  47.815  1.00 23.53           C  
ANISOU 1026  CD2 HIS A 142     2740   3113   3089    -23   -109     31       C  
ATOM   1027  CE1 HIS A 142      14.072  43.957  46.083  1.00 25.62           C  
ANISOU 1027  CE1 HIS A 142     3021   3372   3340    -40   -118      8       C  
ATOM   1028  NE2 HIS A 142      12.851  44.283  46.445  1.00 27.61           N  
ANISOU 1028  NE2 HIS A 142     3257   3639   3595    -34   -120     24       N  
ATOM   1029  N   ILE A 143      15.204  42.622  52.462  1.00 10.78           N  
ANISOU 1029  N   ILE A 143     1154   1432   1509     -7    -68     25       N  
ATOM   1030  CA  ILE A 143      15.978  42.466  53.698  1.00 10.58           C  
ANISOU 1030  CA  ILE A 143     1138   1392   1488      1    -58     25       C  
ATOM   1031  C   ILE A 143      16.677  41.130  53.705  1.00 10.34           C  
ANISOU 1031  C   ILE A 143     1114   1348   1468    -13    -57     15       C  
ATOM   1032  O   ILE A 143      17.915  41.072  53.912  1.00  9.98           O  
ANISOU 1032  O   ILE A 143     1082   1289   1421    -10    -53      6       O  
ATOM   1033  CB  ILE A 143      15.084  42.604  54.946  1.00 10.99           C  
ANISOU 1033  CB  ILE A 143     1180   1449   1545     11    -50     41       C  
ATOM   1034  CG1 ILE A 143      14.530  44.063  55.020  1.00 11.94           C  
ANISOU 1034  CG1 ILE A 143     1298   1581   1656     29    -49     51       C  
ATOM   1035  CG2 ILE A 143      15.872  42.280  56.203  1.00 11.19           C  
ANISOU 1035  CG2 ILE A 143     1216   1462   1576     18    -40     41       C  
ATOM   1036  CD1 ILE A 143      13.453  44.176  56.063  1.00 12.99           C  
ANISOU 1036  CD1 ILE A 143     1418   1723   1793     39    -41     66       C  
ATOM   1037  N   CYS A 144      15.924  40.079  53.412  1.00  9.86           N  
ANISOU 1037  N   CYS A 144     1042   1289   1414    -29    -61     14       N  
ATOM   1038  CA  CYS A 144      16.427  38.708  53.478  1.00  9.69           C  
ANISOU 1038  CA  CYS A 144     1026   1253   1404    -42    -59      5       C  
ATOM   1039  C   CYS A 144      17.521  38.536  52.443  1.00  9.30           C  
ANISOU 1039  C   CYS A 144      990   1195   1349    -48    -63    -12       C  
ATOM   1040  O   CYS A 144      18.568  37.973  52.704  1.00  9.17           O  
ANISOU 1040  O   CYS A 144      984   1163   1336    -47    -58    -19       O  
ATOM   1041  CB  CYS A 144      15.272  37.746  53.196  1.00  9.45           C  
ANISOU 1041  CB  CYS A 144      981   1228   1382    -60    -64      8       C  
ATOM   1042  SG  CYS A 144      15.654  36.037  53.492  1.00 10.93           S  
ANISOU 1042  SG  CYS A 144     1174   1395   1585    -76    -60      1       S  
ATOM   1043  N   TYR A 145      17.273  38.980  51.228  1.00  9.05           N  
ANISOU 1043  N   TYR A 145      957   1175   1309    -53    -72    -17       N  
ATOM   1044  CA  TYR A 145      18.214  38.787  50.130  1.00  9.26           C  
ANISOU 1044  CA  TYR A 145      995   1196   1329    -60    -76    -34       C  
ATOM   1045  C   TYR A 145      19.489  39.622  50.313  1.00  8.78           C  
ANISOU 1045  C   TYR A 145      947   1128   1260    -46    -70    -37       C  
ATOM   1046  O   TYR A 145      20.602  39.178  49.998  1.00  9.59           O  
ANISOU 1046  O   TYR A 145     1061   1221   1364    -48    -68    -49       O  
ATOM   1047  CB  TYR A 145      17.550  39.131  48.806  1.00  9.90           C  
ANISOU 1047  CB  TYR A 145     1069   1293   1399    -69    -86    -37       C  
ATOM   1048  CG  TYR A 145      18.385  38.811  47.600  1.00 11.20           C  
ANISOU 1048  CG  TYR A 145     1246   1455   1557    -78    -90    -55       C  
ATOM   1049  CD1 TYR A 145      18.844  37.534  47.378  1.00 11.17           C  
ANISOU 1049  CD1 TYR A 145     1247   1436   1560    -90    -89    -69       C  
ATOM   1050  CD2 TYR A 145      18.683  39.811  46.651  1.00 11.83           C  
ANISOU 1050  CD2 TYR A 145     1329   1545   1620    -73    -95    -57       C  
ATOM   1051  CE1 TYR A 145      19.637  37.240  46.282  1.00 12.89           C  
ANISOU 1051  CE1 TYR A 145     1477   1651   1771    -97    -91    -86       C  
ATOM   1052  CE2 TYR A 145      19.430  39.503  45.549  1.00 13.57           C  
ANISOU 1052  CE2 TYR A 145     1559   1763   1833    -81    -98    -73       C  
ATOM   1053  CZ  TYR A 145      19.906  38.239  45.383  1.00 13.67           C  
ANISOU 1053  CZ  TYR A 145     1579   1763   1853    -92    -95    -87       C  
ATOM   1054  OH  TYR A 145      20.623  37.946  44.255  1.00 17.38           O  
ANISOU 1054  OH  TYR A 145     2058   2231   2314    -99    -97   -103       O  
ATOM   1055  N   PHE A 146      19.347  40.885  50.738  1.00  8.20           N  
ANISOU 1055  N   PHE A 146      873   1063   1181    -31    -69    -26       N  
ATOM   1056  CA  PHE A 146      20.545  41.676  51.067  1.00  8.40           C  
ANISOU 1056  CA  PHE A 146      911   1081   1200    -19    -64    -28       C  
ATOM   1057  C   PHE A 146      21.368  41.010  52.164  1.00  8.40           C  
ANISOU 1057  C   PHE A 146      917   1067   1209    -15    -56    -29       C  
ATOM   1058  O   PHE A 146      22.599  40.924  52.105  1.00  8.81           O  
ANISOU 1058  O   PHE A 146      978   1109   1260    -13    -53    -38       O  
ATOM   1059  CB  PHE A 146      20.197  43.106  51.437  1.00  9.05           C  
ANISOU 1059  CB  PHE A 146      992   1171   1274     -4    -63    -17       C  
ATOM   1060  CG  PHE A 146      19.738  43.965  50.277  1.00  9.53           C  
ANISOU 1060  CG  PHE A 146     1051   1246   1325     -5    -70    -15       C  
ATOM   1061  CD1 PHE A 146      20.289  43.835  49.038  1.00  9.81           C  
ANISOU 1061  CD1 PHE A 146     1092   1283   1353    -14    -75    -26       C  
ATOM   1062  CD2 PHE A 146      18.788  44.945  50.472  1.00 10.48           C  
ANISOU 1062  CD2 PHE A 146     1165   1377   1441      6    -71     -2       C  
ATOM   1063  CE1 PHE A 146      19.888  44.650  48.021  1.00 11.97           C  
ANISOU 1063  CE1 PHE A 146     1363   1569   1615    -13    -82    -23       C  
ATOM   1064  CE2 PHE A 146      18.348  45.711  49.446  1.00 11.65           C  
ANISOU 1064  CE2 PHE A 146     1310   1537   1579      7    -77      1       C  
ATOM   1065  CZ  PHE A 146      18.927  45.594  48.225  1.00 11.80           C  
ANISOU 1065  CZ  PHE A 146     1335   1558   1591     -3    -83     -9       C  
ATOM   1066  N   LEU A 147      20.699  40.526  53.206  1.00  8.05           N  
ANISOU 1066  N   LEU A 147      864   1020   1173    -14    -52    -20       N  
ATOM   1067  CA  LEU A 147      21.372  39.806  54.283  1.00  8.22           C  
ANISOU 1067  CA  LEU A 147      890   1028   1203    -10    -44    -19       C  
ATOM   1068  C   LEU A 147      22.118  38.617  53.758  1.00  8.12           C  
ANISOU 1068  C   LEU A 147      884   1004   1198    -20    -44    -31       C  
ATOM   1069  O   LEU A 147      23.274  38.360  54.126  1.00  7.78           O  
ANISOU 1069  O   LEU A 147      848    950   1156    -15    -40    -36       O  
ATOM   1070  CB  LEU A 147      20.390  39.419  55.392  1.00  9.20           C  
ANISOU 1070  CB  LEU A 147     1005   1155   1336     -8    -40     -5       C  
ATOM   1071  CG  LEU A 147      21.034  38.675  56.607  1.00 10.26           C  
ANISOU 1071  CG  LEU A 147     1144   1277   1479     -3    -32     -2       C  
ATOM   1072  CD1 LEU A 147      22.046  39.598  57.312  1.00 11.14           C  
ANISOU 1072  CD1 LEU A 147     1265   1386   1581     11    -29     -1       C  
ATOM   1073  CD2 LEU A 147      20.003  38.144  57.614  1.00 10.85           C  
ANISOU 1073  CD2 LEU A 147     1209   1354   1561     -4    -27     12       C  
ATOM   1074  N   TYR A 148      21.453  37.847  52.924  1.00  8.48           N  
ANISOU 1074  N   TYR A 148      924   1050   1247    -35    -49    -37       N  
ATOM   1075  CA  TYR A 148      22.097  36.673  52.311  1.00  8.15           C  
ANISOU 1075  CA  TYR A 148      889    996   1212    -45    -49    -50       C  
ATOM   1076  C   TYR A 148      23.431  37.075  51.614  1.00  8.04           C  
ANISOU 1076  C   TYR A 148      886    979   1189    -40    -48    -62       C  
ATOM   1077  O   TYR A 148      24.454  36.460  51.800  1.00  8.22           O  
ANISOU 1077  O   TYR A 148      916    990   1217    -38    -43    -68       O  
ATOM   1078  CB  TYR A 148      21.138  36.016  51.298  1.00  8.59           C  
ANISOU 1078  CB  TYR A 148      939   1055   1269    -63    -56    -57       C  
ATOM   1079  CG  TYR A 148      21.827  34.941  50.521  1.00  8.36           C  
ANISOU 1079  CG  TYR A 148      920   1014   1245    -73    -55    -74       C  
ATOM   1080  CD1 TYR A 148      22.214  33.775  51.156  1.00  8.34           C  
ANISOU 1080  CD1 TYR A 148      921    991   1255    -75    -49    -75       C  
ATOM   1081  CD2 TYR A 148      22.213  35.137  49.221  1.00  8.03           C  
ANISOU 1081  CD2 TYR A 148      883    976   1192    -78    -60    -88       C  
ATOM   1082  CE1 TYR A 148      22.884  32.759  50.473  1.00  8.41           C  
ANISOU 1082  CE1 TYR A 148      940    987   1269    -82    -47    -91       C  
ATOM   1083  CE2 TYR A 148      22.915  34.168  48.520  1.00  8.18           C  
ANISOU 1083  CE2 TYR A 148      912    982   1214    -86    -58   -104       C  
ATOM   1084  CZ  TYR A 148      23.246  32.962  49.129  1.00  8.25           C  
ANISOU 1084  CZ  TYR A 148      926    972   1238    -87    -51   -106       C  
ATOM   1085  OH  TYR A 148      23.988  31.994  48.460  1.00  8.93           O  
ANISOU 1085  OH  TYR A 148     1022   1043   1327    -93    -48   -123       O  
ATOM   1086  N   GLN A 149      23.377  38.117  50.786  1.00  7.90           N  
ANISOU 1086  N   GLN A 149      869    974   1159    -39    -53    -64       N  
ATOM   1087  CA  GLN A 149      24.566  38.552  50.059  1.00  7.89           C  
ANISOU 1087  CA  GLN A 149      877    973   1149    -36    -53    -74       C  
ATOM   1088  C   GLN A 149      25.649  39.067  50.978  1.00  7.42           C  
ANISOU 1088  C   GLN A 149      822    907   1089    -23    -46    -70       C  
ATOM   1089  O   GLN A 149      26.851  38.852  50.705  1.00  7.24           O  
ANISOU 1089  O   GLN A 149      807    879   1066    -21    -43    -79       O  
ATOM   1090  CB  GLN A 149      24.176  39.590  49.032  1.00  8.02           C  
ANISOU 1090  CB  GLN A 149      892   1004   1151    -38    -59    -75       C  
ATOM   1091  CG  GLN A 149      23.296  39.009  47.907  1.00  8.88           C  
ANISOU 1091  CG  GLN A 149      997   1120   1258    -53    -67    -82       C  
ATOM   1092  CD  GLN A 149      23.023  40.097  46.898  1.00  9.70           C  
ANISOU 1092  CD  GLN A 149     1100   1240   1347    -53    -74    -81       C  
ATOM   1093  OE1 GLN A 149      23.840  40.399  46.039  1.00 10.01           O  
ANISOU 1093  OE1 GLN A 149     1146   1281   1377    -53    -74    -89       O  
ATOM   1094  NE2 GLN A 149      21.933  40.724  47.046  1.00 11.18           N  
ANISOU 1094  NE2 GLN A 149     1278   1438   1532    -50    -78    -69       N  
ATOM   1095  N   ILE A 150      25.293  39.798  52.025  1.00  7.39           N  
ANISOU 1095  N   ILE A 150      816    908   1085    -14    -45    -58       N  
ATOM   1096  CA  ILE A 150      26.296  40.245  53.006  1.00  7.58           C  
ANISOU 1096  CA  ILE A 150      845    927   1109     -3    -40    -54       C  
ATOM   1097  C   ILE A 150      27.009  39.044  53.560  1.00  7.48           C  
ANISOU 1097  C   ILE A 150      833    901   1106     -2    -34    -57       C  
ATOM   1098  O   ILE A 150      28.242  39.019  53.641  1.00  7.69           O  
ANISOU 1098  O   ILE A 150      866    925   1133      2    -31    -62       O  
ATOM   1099  CB  ILE A 150      25.636  41.023  54.160  1.00  7.95           C  
ANISOU 1099  CB  ILE A 150      889    979   1155      7    -38    -40       C  
ATOM   1100  CG1 ILE A 150      25.024  42.364  53.651  1.00  8.20           C  
ANISOU 1100  CG1 ILE A 150      920   1021   1175     10    -42    -37       C  
ATOM   1101  CG2 ILE A 150      26.647  41.309  55.244  1.00  8.30           C  
ANISOU 1101  CG2 ILE A 150      938   1018   1198     17    -34    -38       C  
ATOM   1102  CD1 ILE A 150      24.064  42.999  54.646  1.00  8.34           C  
ANISOU 1102  CD1 ILE A 150      933   1044   1193     19    -40    -24       C  
ATOM   1103  N   LEU A 151      26.247  38.050  53.964  1.00  7.82           N  
ANISOU 1103  N   LEU A 151      872    939   1159     -7    -33    -53       N  
ATOM   1104  CA  LEU A 151      26.802  36.828  54.592  1.00  7.99           C  
ANISOU 1104  CA  LEU A 151      896    947   1193     -6    -28    -53       C  
ATOM   1105  C   LEU A 151      27.604  35.982  53.585  1.00  8.38           C  
ANISOU 1105  C   LEU A 151      951    988   1246    -11    -27    -68       C  
ATOM   1106  O   LEU A 151      28.634  35.385  53.935  1.00  8.18           O  
ANISOU 1106  O   LEU A 151      929    952   1225     -5    -21    -70       O  
ATOM   1107  CB  LEU A 151      25.733  36.015  55.298  1.00  8.83           C  
ANISOU 1107  CB  LEU A 151      996   1048   1310    -10    -26    -44       C  
ATOM   1108  CG  LEU A 151      25.120  36.679  56.549  1.00  9.05           C  
ANISOU 1108  CG  LEU A 151     1019   1084   1336     -1    -24    -28       C  
ATOM   1109  CD1 LEU A 151      23.838  35.917  56.885  1.00 10.66           C  
ANISOU 1109  CD1 LEU A 151     1214   1286   1549     -9    -23    -20       C  
ATOM   1110  CD2 LEU A 151      26.123  36.659  57.688  1.00  9.37           C  
ANISOU 1110  CD2 LEU A 151     1063   1119   1376     11    -19    -23       C  
ATOM   1111  N   ARG A 152      27.117  35.898  52.354  1.00  8.29           N  
ANISOU 1111  N   ARG A 152      939    979   1230    -22    -31    -78       N  
ATOM   1112  CA  ARG A 152      27.821  35.182  51.341  1.00  8.26           C  
ANISOU 1112  CA  ARG A 152      942    968   1227    -28    -30    -93       C  
ATOM   1113  C   ARG A 152      29.238  35.807  51.084  1.00  8.34           C  
ANISOU 1113  C   ARG A 152      958    983   1230    -18    -27    -98       C  
ATOM   1114  O   ARG A 152      30.265  35.131  51.038  1.00  8.66           O  
ANISOU 1114  O   ARG A 152     1002   1013   1274    -14    -21   -104       O  
ATOM   1115  CB  ARG A 152      26.984  35.137  50.031  1.00  8.59           C  
ANISOU 1115  CB  ARG A 152      983   1017   1263    -42    -37   -102       C  
ATOM   1116  CG  ARG A 152      27.578  34.332  48.913  1.00  8.95           C  
ANISOU 1116  CG  ARG A 152     1037   1056   1308    -48    -35   -120       C  
ATOM   1117  CD  ARG A 152      26.615  34.221  47.785  1.00  9.41           C  
ANISOU 1117  CD  ARG A 152     1094   1122   1361    -63    -43   -128       C  
ATOM   1118  NE  ARG A 152      27.113  33.459  46.643  1.00 10.00           N  
ANISOU 1118  NE  ARG A 152     1177   1190   1432    -71    -41   -147       N  
ATOM   1119  CZ  ARG A 152      27.389  33.968  45.464  1.00 11.53           C  
ANISOU 1119  CZ  ARG A 152     1374   1395   1611    -74    -44   -157       C  
ATOM   1120  NH1 ARG A 152      27.426  35.282  45.230  1.00 12.22           N  
ANISOU 1120  NH1 ARG A 152     1458   1499   1686    -69    -48   -150       N  
ATOM   1121  NH2 ARG A 152      27.627  33.120  44.457  1.00 12.46           N  
ANISOU 1121  NH2 ARG A 152     1501   1508   1728    -82    -43   -175       N  
ATOM   1122  N   GLY A 153      29.279  37.143  50.977  1.00  8.08           N  
ANISOU 1122  N   GLY A 153      923    962   1184    -15    -30    -94       N  
ATOM   1123  CA  GLY A 153      30.540  37.867  50.875  1.00  8.16           C  
ANISOU 1123  CA  GLY A 153      937    977   1188     -8    -28    -96       C  
ATOM   1124  C   GLY A 153      31.405  37.666  52.098  1.00  7.60           C  
ANISOU 1124  C   GLY A 153      865    899   1123      3    -23    -89       C  
ATOM   1125  O   GLY A 153      32.621  37.401  51.984  1.00  7.29           O  
ANISOU 1125  O   GLY A 153      827    857   1084      7    -18    -94       O  
ATOM   1126  N   LEU A 154      30.787  37.726  53.276  1.00  7.43           N  
ANISOU 1126  N   LEU A 154      840    876   1106      7    -23    -77       N  
ATOM   1127  CA  LEU A 154      31.543  37.588  54.489  1.00  7.57           C  
ANISOU 1127  CA  LEU A 154      857    890   1127     17    -19    -70       C  
ATOM   1128  C   LEU A 154      32.097  36.193  54.645  1.00  7.64           C  
ANISOU 1128  C   LEU A 154      866    886   1148     19    -14    -72       C  
ATOM   1129  O   LEU A 154      33.158  36.009  55.212  1.00  8.42           O  
ANISOU 1129  O   LEU A 154      966    984   1250     28    -11    -70       O  
ATOM   1130  CB  LEU A 154      30.662  37.944  55.703  1.00  7.59           C  
ANISOU 1130  CB  LEU A 154      857    896   1131     21    -20    -56       C  
ATOM   1131  CG  LEU A 154      31.454  38.154  57.006  1.00  7.79           C  
ANISOU 1131  CG  LEU A 154      882    922   1156     31    -18    -48       C  
ATOM   1132  CD1 LEU A 154      32.458  39.249  56.935  1.00  8.04           C  
ANISOU 1132  CD1 LEU A 154      916    962   1178     34    -20    -51       C  
ATOM   1133  CD2 LEU A 154      30.476  38.436  58.131  1.00  8.18           C  
ANISOU 1133  CD2 LEU A 154      929    974   1205     35    -18    -36       C  
ATOM   1134  N   LYS A 155      31.394  35.162  54.178  1.00  7.92           N  
ANISOU 1134  N   LYS A 155      904    913   1193     12    -13    -77       N  
ATOM   1135  CA  LYS A 155      31.933  33.795  54.233  1.00  8.66           C  
ANISOU 1135  CA  LYS A 155     1001    992   1299     14     -7    -81       C  
ATOM   1136  C   LYS A 155      33.259  33.750  53.458  1.00  8.51           C  
ANISOU 1136  C   LYS A 155      984    973   1276     19     -3    -92       C  
ATOM   1137  O   LYS A 155      34.231  33.165  53.904  1.00  8.92           O  
ANISOU 1137  O   LYS A 155     1037   1019   1335     28      2    -90       O  
ATOM   1138  CB  LYS A 155      30.918  32.796  53.646  1.00  9.18           C  
ANISOU 1138  CB  LYS A 155     1068   1046   1373      2     -7    -86       C  
ATOM   1139  CG  LYS A 155      31.437  31.384  53.637  1.00 10.02           C  
ANISOU 1139  CG  LYS A 155     1180   1135   1493      4      0    -91       C  
ATOM   1140  CD  LYS A 155      30.641  30.414  52.773  1.00 10.70           C  
ANISOU 1140  CD  LYS A 155     1271   1209   1586    -10      0   -102       C  
ATOM   1141  CE  LYS A 155      31.183  28.996  52.875  1.00 11.26           C  
ANISOU 1141  CE  LYS A 155     1350   1258   1672     -6      8   -106       C  
ATOM   1142  NZ  LYS A 155      30.495  28.154  51.903  1.00 12.35           N  
ANISOU 1142  NZ  LYS A 155     1493   1385   1814    -21      7   -120       N  
ATOM   1143  N   TYR A 156      33.295  34.374  52.292  1.00  8.12           N  
ANISOU 1143  N   TYR A 156      937    932   1217     12     -6   -102       N  
ATOM   1144  CA  TYR A 156      34.507  34.419  51.487  1.00  8.06           C  
ANISOU 1144  CA  TYR A 156      931    926   1204     16     -2   -113       C  
ATOM   1145  C   TYR A 156      35.614  35.147  52.256  1.00  8.10           C  
ANISOU 1145  C   TYR A 156      932    941   1206     26     -1   -105       C  
ATOM   1146  O   TYR A 156      36.753  34.650  52.351  1.00  8.34           O  
ANISOU 1146  O   TYR A 156      961    967   1240     35      5   -106       O  
ATOM   1147  CB  TYR A 156      34.230  35.050  50.122  1.00  8.43           C  
ANISOU 1147  CB  TYR A 156      981    984   1239      6     -6   -123       C  
ATOM   1148  CG  TYR A 156      35.407  35.152  49.230  1.00  8.63           C  
ANISOU 1148  CG  TYR A 156     1008   1014   1258      9     -1   -133       C  
ATOM   1149  CD1 TYR A 156      35.811  34.089  48.422  1.00  9.22           C  
ANISOU 1149  CD1 TYR A 156     1087   1079   1336      9      5   -147       C  
ATOM   1150  CD2 TYR A 156      36.165  36.295  49.231  1.00  8.68           C  
ANISOU 1150  CD2 TYR A 156     1011   1033   1255     12     -2   -130       C  
ATOM   1151  CE1 TYR A 156      36.877  34.249  47.555  1.00  9.35           C  
ANISOU 1151  CE1 TYR A 156     1105   1102   1345     12     10   -156       C  
ATOM   1152  CE2 TYR A 156      37.269  36.423  48.365  1.00  9.44           C  
ANISOU 1152  CE2 TYR A 156     1107   1135   1344     14      3   -138       C  
ATOM   1153  CZ  TYR A 156      37.583  35.408  47.543  1.00  9.56           C  
ANISOU 1153  CZ  TYR A 156     1127   1143   1362     14      9   -151       C  
ATOM   1154  OH  TYR A 156      38.687  35.590  46.720  1.00 11.48           O  
ANISOU 1154  OH  TYR A 156     1370   1395   1598     17     15   -159       O  
ATOM   1155  N   ILE A 157      35.306  36.334  52.770  1.00  7.64           N  
ANISOU 1155  N   ILE A 157      871    893   1139     25     -7    -96       N  
ATOM   1156  CA  ILE A 157      36.265  37.146  53.507  1.00  7.67           C  
ANISOU 1156  CA  ILE A 157      872    906   1138     32     -7    -89       C  
ATOM   1157  C   ILE A 157      36.844  36.371  54.698  1.00  7.10           C  
ANISOU 1157  C   ILE A 157      796    827   1076     43     -4    -81       C  
ATOM   1158  O   ILE A 157      38.087  36.236  54.864  1.00  7.43           O  
ANISOU 1158  O   ILE A 157      833    871   1117     50     -1    -81       O  
ATOM   1159  CB  ILE A 157      35.629  38.466  53.933  1.00  7.89           C  
ANISOU 1159  CB  ILE A 157      899    942   1157     29    -13    -82       C  
ATOM   1160  CG1 ILE A 157      35.195  39.309  52.735  1.00  7.91           C  
ANISOU 1160  CG1 ILE A 157      904    951   1149     21    -16    -89       C  
ATOM   1161  CG2 ILE A 157      36.551  39.267  54.813  1.00  7.98           C  
ANISOU 1161  CG2 ILE A 157      908    961   1163     35    -14    -76       C  
ATOM   1162  CD1 ILE A 157      34.286  40.441  53.111  1.00  8.36           C  
ANISOU 1162  CD1 ILE A 157      963   1015   1200     19    -22    -82       C  
ATOM   1163  N   HIS A 158      35.949  35.832  55.512  1.00  7.14           N  
ANISOU 1163  N   HIS A 158      801    824   1087     44     -4    -73       N  
ATOM   1164  CA  HIS A 158      36.358  35.027  56.699  1.00  7.44           C  
ANISOU 1164  CA  HIS A 158      837    856   1134     54     -1    -63       C  
ATOM   1165  C   HIS A 158      37.141  33.789  56.313  1.00  7.96           C  
ANISOU 1165  C   HIS A 158      903    911   1211     60      6    -68       C  
ATOM   1166  O   HIS A 158      37.997  33.349  57.101  1.00  8.33           O  
ANISOU 1166  O   HIS A 158      947    957   1262     71      9    -60       O  
ATOM   1167  CB  HIS A 158      35.157  34.696  57.553  1.00  7.40           C  
ANISOU 1167  CB  HIS A 158      832    846   1135     53     -2    -53       C  
ATOM   1168  CG  HIS A 158      34.738  35.844  58.424  1.00  7.62           C  
ANISOU 1168  CG  HIS A 158      858    884   1152     54     -7    -44       C  
ATOM   1169  ND1 HIS A 158      33.729  35.738  59.369  1.00  7.82           N  
ANISOU 1169  ND1 HIS A 158      883    909   1180     54     -7    -33       N  
ATOM   1170  CD2 HIS A 158      35.134  37.154  58.448  1.00  7.79           C  
ANISOU 1170  CD2 HIS A 158      879    919   1161     53    -11    -45       C  
ATOM   1171  CE1 HIS A 158      33.578  36.900  59.975  1.00  8.06           C  
ANISOU 1171  CE1 HIS A 158      913    950   1199     56    -10    -28       C  
ATOM   1172  NE2 HIS A 158      34.435  37.776  59.448  1.00  7.78           N  
ANISOU 1172  NE2 HIS A 158      878    922   1155     55    -13    -36       N  
ATOM   1173  N   SER A 159      36.857  33.203  55.133  1.00  8.45           N  
ANISOU 1173  N   SER A 159      970    964   1276     54      9    -80       N  
ATOM   1174  CA  SER A 159      37.564  31.984  54.714  1.00  9.02           C  
ANISOU 1174  CA  SER A 159     1045   1024   1358     60     17    -87       C  
ATOM   1175  C   SER A 159      39.048  32.265  54.473  1.00  9.43           C  
ANISOU 1175  C   SER A 159     1093   1086   1407     69     20    -90       C  
ATOM   1176  O   SER A 159      39.859  31.325  54.512  1.00 11.90           O  
ANISOU 1176  O   SER A 159     1404   1389   1727     80     27    -91       O  
ATOM   1177  CB  SER A 159      36.908  31.361  53.478  1.00  9.11           C  
ANISOU 1177  CB  SER A 159     1064   1025   1373     50     19   -102       C  
ATOM   1178  OG  SER A 159      37.219  32.085  52.341  1.00  9.82           O  
ANISOU 1178  OG  SER A 159     1154   1126   1450     44     17   -113       O  
ATOM   1179  N   ALA A 160      39.404  33.541  54.234  1.00  9.62           N  
ANISOU 1179  N   ALA A 160     1112   1126   1417     66     15    -91       N  
ATOM   1180  CA  ALA A 160      40.830  33.943  54.119  1.00  9.57           C  
ANISOU 1180  CA  ALA A 160     1100   1132   1407     73     18    -92       C  
ATOM   1181  C   ALA A 160      41.433  34.368  55.461  1.00  9.88           C  
ANISOU 1181  C   ALA A 160     1130   1179   1444     81     14    -78       C  
ATOM   1182  O   ALA A 160      42.512  34.917  55.526  1.00  9.90           O  
ANISOU 1182  O   ALA A 160     1126   1195   1441     84     14    -76       O  
ATOM   1183  CB  ALA A 160      40.951  35.060  53.096  1.00  9.54           C  
ANISOU 1183  CB  ALA A 160     1095   1140   1389     63     15   -100       C  
ATOM   1184  N   ASN A 161      40.657  34.171  56.526  1.00  9.50           N  
ANISOU 1184  N   ASN A 161     1084   1126   1400     82     11    -67       N  
ATOM   1185  CA  ASN A 161      40.926  34.652  57.883  1.00 10.18           C  
ANISOU 1185  CA  ASN A 161     1165   1222   1483     87      6    -54       C  
ATOM   1186  C   ASN A 161      41.029  36.160  57.978  1.00  9.25           C  
ANISOU 1186  C   ASN A 161     1046   1119   1351     80     -1    -54       C  
ATOM   1187  O   ASN A 161      41.592  36.684  58.934  1.00  9.92           O  
ANISOU 1187  O   ASN A 161     1126   1214   1430     83     -5    -46       O  
ATOM   1188  CB  ASN A 161      42.112  33.974  58.518  1.00 10.94           C  
ANISOU 1188  CB  ASN A 161     1254   1320   1585    101      9    -46       C  
ATOM   1189  CG  ASN A 161      41.875  32.534  58.722  1.00 13.46           C  
ANISOU 1189  CG  ASN A 161     1576   1621   1918    110     16    -42       C  
ATOM   1190  OD1 ASN A 161      40.703  32.047  58.851  1.00 15.14           O  
ANISOU 1190  OD1 ASN A 161     1795   1821   2136    105     17    -41       O  
ATOM   1191  ND2 ASN A 161      42.959  31.788  58.754  1.00 16.24           N  
ANISOU 1191  ND2 ASN A 161     1922   1972   2276    123     21    -40       N  
ATOM   1192  N   VAL A 162      40.387  36.883  57.064  1.00  8.51           N  
ANISOU 1192  N   VAL A 162      957   1026   1250     69     -3    -63       N  
ATOM   1193  CA  VAL A 162      40.347  38.348  57.051  1.00  8.06           C  
ANISOU 1193  CA  VAL A 162      901    982   1182     61     -9    -63       C  
ATOM   1194  C   VAL A 162      39.090  38.758  57.822  1.00  7.75           C  
ANISOU 1194  C   VAL A 162      866    939   1139     59    -13    -57       C  
ATOM   1195  O   VAL A 162      38.005  38.200  57.644  1.00  7.87           O  
ANISOU 1195  O   VAL A 162      885    945   1160     57    -12    -57       O  
ATOM   1196  CB  VAL A 162      40.340  38.886  55.589  1.00  8.06           C  
ANISOU 1196  CB  VAL A 162      904    984   1176     52     -8    -75       C  
ATOM   1197  CG1 VAL A 162      40.066  40.368  55.569  1.00  8.21           C  
ANISOU 1197  CG1 VAL A 162      925   1010   1183     44    -14    -74       C  
ATOM   1198  CG2 VAL A 162      41.653  38.571  54.925  1.00  8.55           C  
ANISOU 1198  CG2 VAL A 162      960   1051   1239     55     -3    -80       C  
ATOM   1199  N   LEU A 163      39.285  39.786  58.641  1.00  7.43           N  
ANISOU 1199  N   LEU A 163      825    908   1090     58    -18    -52       N  
ATOM   1200  CA  LEU A 163      38.242  40.459  59.367  1.00  7.82           C  
ANISOU 1200  CA  LEU A 163      880    958   1135     57    -22    -47       C  
ATOM   1201  C   LEU A 163      38.045  41.783  58.676  1.00  7.90           C  
ANISOU 1201  C   LEU A 163      894    972   1135     48    -25    -52       C  
ATOM   1202  O   LEU A 163      38.991  42.522  58.504  1.00  8.50           O  
ANISOU 1202  O   LEU A 163      970   1055   1205     45    -27    -55       O  
ATOM   1203  CB  LEU A 163      38.692  40.705  60.794  1.00  8.18           C  
ANISOU 1203  CB  LEU A 163      923   1010   1176     63    -25    -38       C  
ATOM   1204  CG  LEU A 163      39.231  39.476  61.519  1.00  9.04           C  
ANISOU 1204  CG  LEU A 163     1026   1116   1292     72    -22    -31       C  
ATOM   1205  CD1 LEU A 163      39.700  39.894  62.919  1.00  9.40           C  
ANISOU 1205  CD1 LEU A 163     1070   1172   1331     77    -26    -22       C  
ATOM   1206  CD2 LEU A 163      38.141  38.399  61.636  1.00  9.59           C  
ANISOU 1206  CD2 LEU A 163     1098   1174   1372     75    -17    -26       C  
ATOM   1207  N   HIS A 164      36.812  42.135  58.348  1.00  7.45           N  
ANISOU 1207  N   HIS A 164      842    911   1076     45    -25    -52       N  
ATOM   1208  CA  HIS A 164      36.534  43.395  57.706  1.00  7.57           C  
ANISOU 1208  CA  HIS A 164      863    931   1083     38    -28    -56       C  
ATOM   1209  C   HIS A 164      36.706  44.569  58.715  1.00  8.07           C  
ANISOU 1209  C   HIS A 164      931    999   1138     39    -31    -52       C  
ATOM   1210  O   HIS A 164      37.338  45.614  58.446  1.00  8.25           O  
ANISOU 1210  O   HIS A 164      956   1025   1153     34    -34    -56       O  
ATOM   1211  CB  HIS A 164      35.124  43.397  57.081  1.00  7.40           C  
ANISOU 1211  CB  HIS A 164      844    905   1063     35    -28    -56       C  
ATOM   1212  CG  HIS A 164      34.783  44.647  56.361  1.00  7.59           C  
ANISOU 1212  CG  HIS A 164      874    933   1078     30    -30    -58       C  
ATOM   1213  ND1 HIS A 164      34.471  45.813  57.023  1.00  7.76           N  
ANISOU 1213  ND1 HIS A 164      901    955   1093     32    -32    -54       N  
ATOM   1214  CD2 HIS A 164      34.682  44.920  55.041  1.00  7.97           C  
ANISOU 1214  CD2 HIS A 164      923    982   1123     24    -31    -64       C  
ATOM   1215  CE1 HIS A 164      34.168  46.754  56.135  1.00  7.62           C  
ANISOU 1215  CE1 HIS A 164      888    939   1069     28    -34    -56       C  
ATOM   1216  NE2 HIS A 164      34.283  46.228  54.929  1.00  7.71           N  
ANISOU 1216  NE2 HIS A 164      896    951   1082     23    -33    -61       N  
ATOM   1217  N   ARG A 165      35.978  44.435  59.829  1.00  8.70           N  
ANISOU 1217  N   ARG A 165     1012   1077   1218     45    -31    -45       N  
ATOM   1218  CA  ARG A 165      36.031  45.321  61.006  1.00  9.79           C  
ANISOU 1218  CA  ARG A 165     1154   1218   1347     48    -34    -42       C  
ATOM   1219  C   ARG A 165      35.397  46.680  60.826  1.00 10.31           C  
ANISOU 1219  C   ARG A 165     1229   1283   1405     46    -35    -44       C  
ATOM   1220  O   ARG A 165      35.482  47.486  61.766  1.00 12.14           O  
ANISOU 1220  O   ARG A 165     1466   1517   1629     47    -37    -43       O  
ATOM   1221  CB  ARG A 165      37.464  45.506  61.492  1.00 10.06           C  
ANISOU 1221  CB  ARG A 165     1186   1259   1377     47    -37    -44       C  
ATOM   1222  CG  ARG A 165      38.102  44.206  61.941  1.00 10.99           C  
ANISOU 1222  CG  ARG A 165     1295   1379   1503     53    -36    -39       C  
ATOM   1223  CD  ARG A 165      39.571  44.273  62.223  1.00 12.35           C  
ANISOU 1223  CD  ARG A 165     1461   1559   1672     51    -39    -41       C  
ATOM   1224  NE  ARG A 165      39.848  44.819  63.571  1.00 16.17           N  
ANISOU 1224  NE  ARG A 165     1947   2050   2147     53    -43    -37       N  
ATOM   1225  CZ  ARG A 165      40.395  45.983  63.796  1.00 17.50           C  
ANISOU 1225  CZ  ARG A 165     2120   2224   2305     46    -48    -41       C  
ATOM   1226  NH1 ARG A 165      40.647  46.376  65.029  1.00 21.70           N  
ANISOU 1226  NH1 ARG A 165     2654   2762   2828     48    -53    -39       N  
ATOM   1227  NH2 ARG A 165      40.677  46.759  62.818  1.00 21.82           N  
ANISOU 1227  NH2 ARG A 165     2669   2769   2851     37    -48    -48       N  
ATOM   1228  N   ASP A 166      34.699  46.943  59.725  1.00  9.22           N  
ANISOU 1228  N   ASP A 166     1093   1142   1268     42    -34    -46       N  
ATOM   1229  CA  ASP A 166      33.973  48.218  59.642  1.00  9.27           C  
ANISOU 1229  CA  ASP A 166     1107   1147   1267     42    -35    -45       C  
ATOM   1230  C   ASP A 166      32.723  48.055  58.829  1.00  8.11           C  
ANISOU 1230  C   ASP A 166      960    999   1124     43    -33    -43       C  
ATOM   1231  O   ASP A 166      32.365  48.970  58.030  1.00  8.42           O  
ANISOU 1231  O   ASP A 166     1003   1036   1158     41    -34    -44       O  
ATOM   1232  CB  ASP A 166      34.866  49.341  59.123  1.00  9.77           C  
ANISOU 1232  CB  ASP A 166     1177   1210   1324     35    -37    -50       C  
ATOM   1233  CG  ASP A 166      34.409  50.726  59.546  1.00 10.62           C  
ANISOU 1233  CG  ASP A 166     1297   1315   1425     37    -38    -50       C  
ATOM   1234  OD1 ASP A 166      33.553  50.927  60.425  1.00 10.13           O  
ANISOU 1234  OD1 ASP A 166     1238   1250   1360     45    -36    -46       O  
ATOM   1235  OD2 ASP A 166      35.011  51.698  58.966  1.00 11.93           O  
ANISOU 1235  OD2 ASP A 166     1469   1479   1586     29    -39    -53       O  
ATOM   1236  N   LEU A 167      32.022  46.918  58.967  1.00  7.74           N  
ANISOU 1236  N   LEU A 167      905    951   1084     46    -32    -39       N  
ATOM   1237  CA  LEU A 167      30.766  46.696  58.234  1.00  8.20           C  
ANISOU 1237  CA  LEU A 167      959   1009   1146     46    -31    -36       C  
ATOM   1238  C   LEU A 167      29.701  47.650  58.734  1.00  8.36           C  
ANISOU 1238  C   LEU A 167      985   1031   1162     52    -30    -30       C  
ATOM   1239  O   LEU A 167      29.498  47.822  59.954  1.00  8.38           O  
ANISOU 1239  O   LEU A 167      989   1033   1161     60    -28    -26       O  
ATOM   1240  CB  LEU A 167      30.297  45.235  58.330  1.00  8.30           C  
ANISOU 1240  CB  LEU A 167      964   1020   1168     45    -30    -34       C  
ATOM   1241  CG  LEU A 167      31.227  44.223  57.677  1.00  8.82           C  
ANISOU 1241  CG  LEU A 167     1027   1084   1241     40    -29    -41       C  
ATOM   1242  CD1 LEU A 167      30.854  42.822  58.142  1.00  8.82           C  
ANISOU 1242  CD1 LEU A 167     1021   1080   1251     41    -27    -37       C  
ATOM   1243  CD2 LEU A 167      31.173  44.353  56.162  1.00  9.34           C  
ANISOU 1243  CD2 LEU A 167     1093   1151   1304     32    -32    -48       C  
ATOM   1244  N   LYS A 168      29.018  48.297  57.796  1.00  8.04           N  
ANISOU 1244  N   LYS A 168      944    991   1118     51    -32    -29       N  
ATOM   1245  CA  LYS A 168      27.965  49.241  58.111  1.00  8.86           C  
ANISOU 1245  CA  LYS A 168     1052   1097   1218     59    -30    -23       C  
ATOM   1246  C   LYS A 168      27.247  49.549  56.764  1.00  8.26           C  
ANISOU 1246  C   LYS A 168      973   1024   1140     56    -33    -22       C  
ATOM   1247  O   LYS A 168      27.737  49.195  55.692  1.00  7.84           O  
ANISOU 1247  O   LYS A 168      919    972   1089     48    -36    -27       O  
ATOM   1248  CB  LYS A 168      28.512  50.519  58.719  1.00  9.14           C  
ANISOU 1248  CB  LYS A 168     1099   1128   1245     63    -29    -25       C  
ATOM   1249  CG  LYS A 168      29.549  51.214  57.889  1.00  9.86           C  
ANISOU 1249  CG  LYS A 168     1198   1217   1333     56    -32    -31       C  
ATOM   1250  CD  LYS A 168      30.031  52.432  58.628  1.00 10.28           C  
ANISOU 1250  CD  LYS A 168     1264   1265   1379     58    -31    -33       C  
ATOM   1251  CE  LYS A 168      31.107  53.123  57.897  1.00 11.22           C  
ANISOU 1251  CE  LYS A 168     1389   1380   1494     49    -33    -38       C  
ATOM   1252  NZ  LYS A 168      31.399  54.388  58.601  1.00 11.66           N  
ANISOU 1252  NZ  LYS A 168     1458   1429   1543     51    -32    -40       N  
ATOM   1253  N   PRO A 169      26.062  50.167  56.813  1.00  8.33           N  
ANISOU 1253  N   PRO A 169      981   1035   1147     64    -32    -14       N  
ATOM   1254  CA  PRO A 169      25.296  50.293  55.565  1.00  8.48           C  
ANISOU 1254  CA  PRO A 169      995   1060   1166     62    -36    -11       C  
ATOM   1255  C   PRO A 169      26.009  51.028  54.423  1.00  8.54           C  
ANISOU 1255  C   PRO A 169     1010   1068   1168     56    -39    -16       C  
ATOM   1256  O   PRO A 169      25.897  50.612  53.279  1.00  8.85           O  
ANISOU 1256  O   PRO A 169     1044   1112   1207     48    -43    -18       O  
ATOM   1257  CB  PRO A 169      24.024  51.020  56.016  1.00  8.46           C  
ANISOU 1257  CB  PRO A 169      991   1061   1162     74    -33     -1       C  
ATOM   1258  CG  PRO A 169      23.853  50.521  57.418  1.00  8.91           C  
ANISOU 1258  CG  PRO A 169     1046   1117   1223     80    -28      1       C  
ATOM   1259  CD  PRO A 169      25.247  50.508  57.982  1.00  8.57           C  
ANISOU 1259  CD  PRO A 169     1013   1067   1178     76    -27     -7       C  
ATOM   1260  N   SER A 170      26.798  52.072  54.734  1.00  8.54           N  
ANISOU 1260  N   SER A 170     1022   1060   1163     58    -37    -18       N  
ATOM   1261  CA  SER A 170      27.495  52.829  53.723  1.00  8.82           C  
ANISOU 1261  CA  SER A 170     1065   1094   1193     52    -39    -20       C  
ATOM   1262  C   SER A 170      28.632  52.052  53.072  1.00  8.54           C  
ANISOU 1262  C   SER A 170     1027   1060   1158     40    -41    -29       C  
ATOM   1263  O   SER A 170      29.109  52.491  52.026  1.00  9.93           O  
ANISOU 1263  O   SER A 170     1206   1237   1329     34    -42    -30       O  
ATOM   1264  CB  SER A 170      27.913  54.169  54.275  1.00  9.56           C  
ANISOU 1264  CB  SER A 170     1172   1178   1281     57    -36    -19       C  
ATOM   1265  OG  SER A 170      28.823  53.992  55.327  1.00 10.37           O  
ANISOU 1265  OG  SER A 170     1278   1276   1385     55    -34    -25       O  
ATOM   1266  N   ASN A 171      29.024  50.910  53.648  1.00  8.04           N  
ANISOU 1266  N   ASN A 171      958    997   1101     38    -40    -34       N  
ATOM   1267  CA  ASN A 171      30.019  50.059  53.009  1.00  7.97           C  
ANISOU 1267  CA  ASN A 171      945    990   1094     28    -40    -42       C  
ATOM   1268  C   ASN A 171      29.432  48.869  52.283  1.00  8.24           C  
ANISOU 1268  C   ASN A 171      970   1028   1132     24    -42    -44       C  
ATOM   1269  O   ASN A 171      30.137  47.913  51.972  1.00  8.26           O  
ANISOU 1269  O   ASN A 171      970   1031   1138     18    -42    -51       O  
ATOM   1270  CB  ASN A 171      31.063  49.587  54.034  1.00  8.41           C  
ANISOU 1270  CB  ASN A 171     1001   1042   1153     28    -38    -46       C  
ATOM   1271  CG  ASN A 171      31.987  50.716  54.481  1.00  8.55           C  
ANISOU 1271  CG  ASN A 171     1028   1056   1166     27    -38    -47       C  
ATOM   1272  OD1 ASN A 171      32.138  51.737  53.737  1.00  9.21           O  
ANISOU 1272  OD1 ASN A 171     1118   1138   1243     24    -38    -46       O  
ATOM   1273  ND2 ASN A 171      32.567  50.614  55.682  1.00  8.45           N  
ANISOU 1273  ND2 ASN A 171     1016   1040   1154     30    -37    -48       N  
ATOM   1274  N   LEU A 172      28.143  48.920  51.976  1.00  7.93           N  
ANISOU 1274  N   LEU A 172      927    994   1093     27    -45    -38       N  
ATOM   1275  CA  LEU A 172      27.473  47.842  51.241  1.00  8.26           C  
ANISOU 1275  CA  LEU A 172      959   1040   1137     20    -48    -41       C  
ATOM   1276  C   LEU A 172      26.896  48.539  50.002  1.00  8.20           C  
ANISOU 1276  C   LEU A 172      952   1041   1121     18    -52    -38       C  
ATOM   1277  O   LEU A 172      25.891  49.261  50.045  1.00  8.21           O  
ANISOU 1277  O   LEU A 172      952   1046   1120     25    -54    -29       O  
ATOM   1278  CB  LEU A 172      26.360  47.250  52.120  1.00  7.92           C  
ANISOU 1278  CB  LEU A 172      909    999   1103     25    -47    -34       C  
ATOM   1279  CG  LEU A 172      26.878  46.638  53.410  1.00  7.79           C  
ANISOU 1279  CG  LEU A 172      892    974   1093     28    -42    -35       C  
ATOM   1280  CD1 LEU A 172      25.699  46.148  54.182  1.00  8.23           C  
ANISOU 1280  CD1 LEU A 172      941   1032   1155     32    -41    -27       C  
ATOM   1281  CD2 LEU A 172      27.857  45.495  53.213  1.00  7.66           C  
ANISOU 1281  CD2 LEU A 172      876    954   1082     21    -41    -44       C  
ATOM   1282  N   LEU A 173      27.491  48.234  48.860  1.00  7.53           N  
ANISOU 1282  N   LEU A 173      869    960   1032     10    -54    -46       N  
ATOM   1283  CA  LEU A 173      27.156  48.886  47.611  1.00  7.80           C  
ANISOU 1283  CA  LEU A 173      904   1002   1056      7    -58    -43       C  
ATOM   1284  C   LEU A 173      26.116  48.042  46.889  1.00  8.22           C  
ANISOU 1284  C   LEU A 173      949   1065   1110      1    -63    -45       C  
ATOM   1285  O   LEU A 173      26.154  46.773  46.941  1.00  8.56           O  
ANISOU 1285  O   LEU A 173      987   1106   1159     -5    -63    -53       O  
ATOM   1286  CB  LEU A 173      28.406  48.950  46.736  1.00  8.23           C  
ANISOU 1286  CB  LEU A 173      965   1057   1104      0    -56    -51       C  
ATOM   1287  CG  LEU A 173      29.606  49.651  47.330  1.00  8.42           C  
ANISOU 1287  CG  LEU A 173      996   1073   1128      2    -51    -52       C  
ATOM   1288  CD1 LEU A 173      30.795  49.602  46.368  1.00  8.69           C  
ANISOU 1288  CD1 LEU A 173     1034   1111   1156     -5    -48    -59       C  
ATOM   1289  CD2 LEU A 173      29.327  51.043  47.787  1.00  8.88           C  
ANISOU 1289  CD2 LEU A 173     1061   1128   1183     10    -50    -41       C  
ATOM   1290  N   ILE A 174      25.180  48.696  46.189  1.00  8.83           N  
ANISOU 1290  N   ILE A 174     1023   1152   1179      3    -69    -37       N  
ATOM   1291  CA  ILE A 174      24.021  47.987  45.594  1.00  9.80           C  
ANISOU 1291  CA  ILE A 174     1135   1286   1302     -3    -76    -37       C  
ATOM   1292  C   ILE A 174      23.800  48.502  44.177  1.00 11.36           C  
ANISOU 1292  C   ILE A 174     1333   1496   1486     -7    -82    -35       C  
ATOM   1293  O   ILE A 174      23.939  49.695  43.939  1.00 10.47           O  
ANISOU 1293  O   ILE A 174     1227   1386   1367      0    -81    -26       O  
ATOM   1294  CB  ILE A 174      22.741  48.143  46.467  1.00 10.97           C  
ANISOU 1294  CB  ILE A 174     1275   1438   1457      5    -77    -25       C  
ATOM   1295  CG1 ILE A 174      22.966  47.657  47.893  1.00 11.08           C  
ANISOU 1295  CG1 ILE A 174     1288   1439   1482      9    -70    -25       C  
ATOM   1296  CG2 ILE A 174      21.560  47.488  45.819  1.00 11.37           C  
ANISOU 1296  CG2 ILE A 174     1312   1500   1506     -2    -85    -24       C  
ATOM   1297  CD1 ILE A 174      21.941  48.080  48.906  1.00 12.49           C  
ANISOU 1297  CD1 ILE A 174     1461   1620   1666     20    -68    -13       C  
ATOM   1298  N   ASN A 175      23.501  47.606  43.253  1.00 13.39           N  
ANISOU 1298  N   ASN A 175     1586   1762   1739    -18    -87    -43       N  
ATOM   1299  CA  ASN A 175      23.225  47.999  41.844  1.00 16.01           C  
ANISOU 1299  CA  ASN A 175     1917   2109   2055    -23    -94    -42       C  
ATOM   1300  C   ASN A 175      21.775  47.858  41.509  1.00 17.88           C  
ANISOU 1300  C   ASN A 175     2142   2361   2291    -25   -104    -35       C  
ATOM   1301  O   ASN A 175      20.943  47.535  42.394  1.00 18.03           O  
ANISOU 1301  O   ASN A 175     2151   2378   2320    -22   -104    -30       O  
ATOM   1302  CB  ASN A 175      24.161  47.329  40.859  1.00 16.65           C  
ANISOU 1302  CB  ASN A 175     2005   2191   2129    -34    -94    -58       C  
ATOM   1303  CG  ASN A 175      23.882  45.854  40.707  1.00 17.50           C  
ANISOU 1303  CG  ASN A 175     2107   2299   2242    -46    -96    -71       C  
ATOM   1304  OD1 ASN A 175      22.860  45.346  41.188  1.00 17.98           O  
ANISOU 1304  OD1 ASN A 175     2159   2362   2312    -48   -101    -68       O  
ATOM   1305  ND2 ASN A 175      24.794  45.146  40.059  1.00 20.16           N  
ANISOU 1305  ND2 ASN A 175     2451   2633   2576    -53    -93    -86       N  
ATOM   1306  N   THR A 176      21.418  48.133  40.238  1.00 21.05           N  
ANISOU 1306  N   THR A 176     2542   2779   2678    -29   -112    -33       N  
ATOM   1307  CA  THR A 176      20.007  48.160  39.869  1.00 24.04           C  
ANISOU 1307  CA  THR A 176     2907   3175   3053    -30   -122    -24       C  
ATOM   1308  C   THR A 176      19.346  46.780  39.808  1.00 26.09           C  
ANISOU 1308  C   THR A 176     3156   3438   3317    -45   -128    -35       C  
ATOM   1309  O   THR A 176      18.117  46.690  39.838  1.00 26.87           O  
ANISOU 1309  O   THR A 176     3242   3551   3418    -46   -136    -26       O  
ATOM   1310  CB  THR A 176      19.805  48.843  38.508  1.00 26.08           C  
ANISOU 1310  CB  THR A 176     3166   3451   3292    -31   -130    -18       C  
ATOM   1311  OG1 THR A 176      20.628  48.208  37.541  1.00 27.39           O  
ANISOU 1311  OG1 THR A 176     3340   3619   3449    -44   -130    -35       O  
ATOM   1312  CG2 THR A 176      20.156  50.351  38.610  1.00 27.86           C  
ANISOU 1312  CG2 THR A 176     3400   3671   3513    -16   -124     -3       C  
ATOM   1313  N   THR A 177      20.140  45.714  39.766  1.00 23.00           N  
ANISOU 1313  N   THR A 177     2771   3036   2930    -56   -124    -52       N  
ATOM   1314  CA  THR A 177      19.583  44.369  39.885  1.00 25.71           C  
ANISOU 1314  CA  THR A 177     3107   3378   3282    -70   -128    -63       C  
ATOM   1315  C   THR A 177      19.650  43.802  41.339  1.00 21.94           C  
ANISOU 1315  C   THR A 177     2628   2884   2824    -66   -120    -62       C  
ATOM   1316  O   THR A 177      19.426  42.604  41.546  1.00 22.90           O  
ANISOU 1316  O   THR A 177     2747   2999   2955    -77   -121    -71       O  
ATOM   1317  CB  THR A 177      20.257  43.412  38.879  1.00 27.73           C  
ANISOU 1317  CB  THR A 177     3372   3634   3531    -84   -130    -83       C  
ATOM   1318  OG1 THR A 177      21.657  43.624  38.872  1.00 31.23           O  
ANISOU 1318  OG1 THR A 177     3828   4065   3972    -79   -120    -90       O  
ATOM   1319  CG2 THR A 177      19.733  43.701  37.457  1.00 31.62           C  
ANISOU 1319  CG2 THR A 177     3861   4149   4004    -92   -141    -84       C  
ATOM   1320  N   CYS A 178      19.871  44.682  42.325  1.00 19.39           N  
ANISOU 1320  N   CYS A 178     2307   2553   2507    -50   -113    -50       N  
ATOM   1321  CA  CYS A 178      19.901  44.346  43.767  1.00 20.43           C  
ANISOU 1321  CA  CYS A 178     2437   2670   2654    -44   -105    -46       C  
ATOM   1322  C   CYS A 178      21.098  43.461  44.138  1.00 15.98           C  
ANISOU 1322  C   CYS A 178     1884   2089   2098    -48    -97    -60       C  
ATOM   1323  O   CYS A 178      21.107  42.834  45.217  1.00 15.58           O  
ANISOU 1323  O   CYS A 178     1831   2027   2061    -47    -92    -59       O  
ATOM   1324  CB  CYS A 178      18.622  43.714  44.281  1.00 22.69           C  
ANISOU 1324  CB  CYS A 178     2708   2962   2950    -49   -109    -40       C  
ATOM   1325  SG  CYS A 178      17.229  44.874  44.231  1.00 31.52           S  
ANISOU 1325  SG  CYS A 178     3813   4101   4063    -38   -115    -19       S  
ATOM   1326  N   ASP A 179      22.117  43.440  43.293  1.00 14.10           N  
ANISOU 1326  N   ASP A 179     1656   1849   1852    -52    -96    -71       N  
ATOM   1327  CA  ASP A 179      23.389  42.816  43.648  1.00 13.35           C  
ANISOU 1327  CA  ASP A 179     1571   1739   1764    -52    -87    -83       C  
ATOM   1328  C   ASP A 179      24.078  43.707  44.684  1.00 11.70           C  
ANISOU 1328  C   ASP A 179     1366   1521   1557    -38    -80    -74       C  
ATOM   1329  O   ASP A 179      24.052  44.948  44.602  1.00 13.04           O  
ANISOU 1329  O   ASP A 179     1538   1697   1720    -30    -80    -64       O  
ATOM   1330  CB  ASP A 179      24.336  42.749  42.462  1.00 15.04           C  
ANISOU 1330  CB  ASP A 179     1794   1956   1966    -57    -87    -95       C  
ATOM   1331  CG  ASP A 179      23.813  41.926  41.327  1.00 17.75           C  
ANISOU 1331  CG  ASP A 179     2135   2308   2303    -71    -94   -107       C  
ATOM   1332  OD1 ASP A 179      23.105  40.921  41.564  1.00 18.25           O  
ANISOU 1332  OD1 ASP A 179     2193   2367   2375    -80    -97   -111       O  
ATOM   1333  OD2 ASP A 179      24.234  42.254  40.183  1.00 22.10           O  
ANISOU 1333  OD2 ASP A 179     2692   2868   2839    -75    -96   -113       O  
ATOM   1334  N   LEU A 180      24.629  43.079  45.689  1.00  9.82           N  
ANISOU 1334  N   LEU A 180     1130   1270   1332    -35    -73    -76       N  
ATOM   1335  CA  LEU A 180      25.289  43.760  46.807  1.00  9.08           C  
ANISOU 1335  CA  LEU A 180     1040   1168   1241    -23    -66    -69       C  
ATOM   1336  C   LEU A 180      26.764  43.381  46.893  1.00  8.65           C  
ANISOU 1336  C   LEU A 180      993   1104   1189    -23    -60    -79       C  
ATOM   1337  O   LEU A 180      27.121  42.235  46.725  1.00  9.29           O  
ANISOU 1337  O   LEU A 180     1075   1179   1276    -29    -58    -89       O  
ATOM   1338  CB  LEU A 180      24.567  43.401  48.091  1.00  8.93           C  
ANISOU 1338  CB  LEU A 180     1014   1144   1234    -19    -64    -61       C  
ATOM   1339  CG  LEU A 180      25.129  44.024  49.386  1.00  9.03           C  
ANISOU 1339  CG  LEU A 180     1031   1149   1250     -7    -58    -53       C  
ATOM   1340  CD1 LEU A 180      23.969  44.215  50.366  1.00  9.65           C  
ANISOU 1340  CD1 LEU A 180     1102   1230   1334      0    -58    -41       C  
ATOM   1341  CD2 LEU A 180      26.201  43.139  50.031  1.00  9.60           C  
ANISOU 1341  CD2 LEU A 180     1107   1209   1331     -7    -52    -60       C  
ATOM   1342  N   LYS A 181      27.615  44.400  47.067  1.00  8.05           N  
ANISOU 1342  N   LYS A 181      924   1028   1108    -16    -57    -75       N  
ATOM   1343  CA  LYS A 181      29.056  44.198  47.221  1.00  8.26           C  
ANISOU 1343  CA  LYS A 181      956   1048   1137    -15    -51    -82       C  
ATOM   1344  C   LYS A 181      29.578  44.950  48.439  1.00  7.84           C  
ANISOU 1344  C   LYS A 181      905    989   1086     -6    -47    -75       C  
ATOM   1345  O   LYS A 181      29.342  46.141  48.602  1.00  8.16           O  
ANISOU 1345  O   LYS A 181      947   1032   1120     -2    -48    -67       O  
ATOM   1346  CB  LYS A 181      29.784  44.671  45.995  1.00  8.86           C  
ANISOU 1346  CB  LYS A 181     1036   1130   1200    -19    -50    -88       C  
ATOM   1347  CG  LYS A 181      29.476  43.885  44.737  1.00  9.76           C  
ANISOU 1347  CG  LYS A 181     1149   1249   1309    -28    -53    -98       C  
ATOM   1348  CD  LYS A 181      30.183  44.470  43.532  1.00 10.88           C  
ANISOU 1348  CD  LYS A 181     1297   1400   1438    -32    -52   -103       C  
ATOM   1349  CE  LYS A 181      29.707  43.912  42.248  1.00 12.12           C  
ANISOU 1349  CE  LYS A 181     1453   1565   1585    -41    -57   -112       C  
ATOM   1350  NZ  LYS A 181      29.916  42.466  42.076  1.00 13.76           N  
ANISOU 1350  NZ  LYS A 181     1662   1767   1800    -46    -54   -126       N  
ATOM   1351  N   ILE A 182      30.348  44.245  49.227  1.00  7.82           N  
ANISOU 1351  N   ILE A 182      901    978   1091     -4    -43    -78       N  
ATOM   1352  CA  ILE A 182      31.027  44.796  50.372  1.00  7.37           C  
ANISOU 1352  CA  ILE A 182      846    917   1036      3    -40    -73       C  
ATOM   1353  C   ILE A 182      32.256  45.578  49.964  1.00  7.41           C  
ANISOU 1353  C   ILE A 182      856    925   1034      2    -38    -76       C  
ATOM   1354  O   ILE A 182      33.046  45.116  49.168  1.00  6.76           O  
ANISOU 1354  O   ILE A 182      774    844    951     -2    -35    -84       O  
ATOM   1355  CB  ILE A 182      31.435  43.700  51.365  1.00  7.52           C  
ANISOU 1355  CB  ILE A 182      862    928   1066      7    -36    -74       C  
ATOM   1356  CG1 ILE A 182      30.227  42.950  51.929  1.00  7.79           C  
ANISOU 1356  CG1 ILE A 182      892    960   1109      7    -37    -69       C  
ATOM   1357  CG2 ILE A 182      32.284  44.297  52.509  1.00  7.87           C  
ANISOU 1357  CG2 ILE A 182      909    971   1110     13    -34    -69       C  
ATOM   1358  CD1 ILE A 182      30.593  41.621  52.488  1.00  7.77           C  
ANISOU 1358  CD1 ILE A 182      887    949   1117      8    -33    -71       C  
ATOM   1359  N   CYS A 183      32.417  46.763  50.525  1.00  7.18           N  
ANISOU 1359  N   CYS A 183      832    896   1001      6    -38    -69       N  
ATOM   1360  CA  CYS A 183      33.601  47.620  50.234  1.00  7.89           C  
ANISOU 1360  CA  CYS A 183      926    987   1084      3    -36    -71       C  
ATOM   1361  C   CYS A 183      34.273  48.082  51.547  1.00  7.86           C  
ANISOU 1361  C   CYS A 183      924    979   1083      7    -35    -68       C  
ATOM   1362  O   CYS A 183      33.744  47.904  52.654  1.00  8.31           O  
ANISOU 1362  O   CYS A 183      980   1033   1145     13    -36    -63       O  
ATOM   1363  CB  CYS A 183      33.253  48.807  49.330  1.00  8.06           C  
ANISOU 1363  CB  CYS A 183      953   1012   1096      0    -38    -67       C  
ATOM   1364  SG  CYS A 183      32.306  50.140  50.104  1.00  8.99           S  
ANISOU 1364  SG  CYS A 183     1078   1127   1212      7    -41    -56       S  
ATOM   1365  N   ASP A 184      35.446  48.720  51.370  1.00  7.93           N  
ANISOU 1365  N   ASP A 184      935    990   1088      3    -34    -70       N  
ATOM   1366  CA  ASP A 184      36.243  49.415  52.407  1.00  8.12           C  
ANISOU 1366  CA  ASP A 184      962   1012   1111      3    -34    -68       C  
ATOM   1367  C   ASP A 184      36.923  48.437  53.376  1.00  7.83           C  
ANISOU 1367  C   ASP A 184      918    975   1081      7    -33    -69       C  
ATOM   1368  O   ASP A 184      36.393  48.104  54.469  1.00  8.44           O  
ANISOU 1368  O   ASP A 184      996   1050   1163     13    -34    -66       O  
ATOM   1369  CB  ASP A 184      35.483  50.460  53.211  1.00  8.92           C  
ANISOU 1369  CB  ASP A 184     1071   1108   1209      7    -36    -62       C  
ATOM   1370  CG  ASP A 184      36.448  51.455  53.879  1.00  9.80           C  
ANISOU 1370  CG  ASP A 184     1188   1218   1317      3    -37    -62       C  
ATOM   1371  OD1 ASP A 184      37.659  51.068  54.006  1.00  8.98           O  
ANISOU 1371  OD1 ASP A 184     1079   1119   1215     -1    -36    -66       O  
ATOM   1372  OD2 ASP A 184      36.006  52.596  54.290  1.00 11.30           O  
ANISOU 1372  OD2 ASP A 184     1388   1402   1503      5    -38    -58       O  
ATOM   1373  N   PHE A 185      38.104  47.998  52.995  1.00  7.90           N  
ANISOU 1373  N   PHE A 185      922    988   1091      3    -31    -74       N  
ATOM   1374  CA  PHE A 185      38.910  47.093  53.784  1.00  8.05           C  
ANISOU 1374  CA  PHE A 185      934   1009   1117      8    -30    -75       C  
ATOM   1375  C   PHE A 185      40.083  47.823  54.460  1.00  8.14           C  
ANISOU 1375  C   PHE A 185      944   1025   1124      4    -31    -74       C  
ATOM   1376  O   PHE A 185      41.078  47.189  54.878  1.00  7.88           O  
ANISOU 1376  O   PHE A 185      902    996   1095      6    -30    -74       O  
ATOM   1377  CB  PHE A 185      39.399  45.945  52.904  1.00  8.18           C  
ANISOU 1377  CB  PHE A 185      944   1027   1138      8    -25    -81       C  
ATOM   1378  CG  PHE A 185      38.305  44.952  52.570  1.00  8.16           C  
ANISOU 1378  CG  PHE A 185      942   1019   1141     11    -24    -82       C  
ATOM   1379  CD1 PHE A 185      37.336  45.268  51.648  1.00  8.22           C  
ANISOU 1379  CD1 PHE A 185      953   1026   1143      7    -25    -84       C  
ATOM   1380  CD2 PHE A 185      38.168  43.765  53.289  1.00  8.61           C  
ANISOU 1380  CD2 PHE A 185      995   1071   1207     18    -23    -81       C  
ATOM   1381  CE1 PHE A 185      36.296  44.400  51.335  1.00  8.10           C  
ANISOU 1381  CE1 PHE A 185      938   1007   1133      8    -26    -85       C  
ATOM   1382  CE2 PHE A 185      37.141  42.895  52.973  1.00  8.32           C  
ANISOU 1382  CE2 PHE A 185      958   1027   1174     19    -22    -83       C  
ATOM   1383  CZ  PHE A 185      36.225  43.222  51.978  1.00  7.99           C  
ANISOU 1383  CZ  PHE A 185      921    987   1129     13    -24    -86       C  
ATOM   1384  N   GLY A 186      39.969  49.144  54.667  1.00  8.17           N  
ANISOU 1384  N   GLY A 186      955   1027   1121     -1    -34    -72       N  
ATOM   1385  CA  GLY A 186      41.067  49.906  55.262  1.00  8.48           C  
ANISOU 1385  CA  GLY A 186      994   1070   1157     -7    -37    -72       C  
ATOM   1386  C   GLY A 186      41.394  49.500  56.688  1.00  8.87           C  
ANISOU 1386  C   GLY A 186     1039   1122   1208     -2    -40    -70       C  
ATOM   1387  O   GLY A 186      42.538  49.717  57.113  1.00  9.44           O  
ANISOU 1387  O   GLY A 186     1106   1201   1278     -7    -42    -70       O  
ATOM   1388  N   LEU A 187      40.430  49.000  57.429  1.00  8.58           N  
ANISOU 1388  N   LEU A 187     1005   1080   1173      7    -40    -67       N  
ATOM   1389  CA  LEU A 187      40.647  48.575  58.827  1.00  9.23           C  
ANISOU 1389  CA  LEU A 187     1085   1166   1257     13    -43    -64       C  
ATOM   1390  C   LEU A 187      40.725  47.096  58.939  1.00  8.73           C  
ANISOU 1390  C   LEU A 187     1012   1104   1202     21    -40    -61       C  
ATOM   1391  O   LEU A 187      40.735  46.530  60.043  1.00  9.58           O  
ANISOU 1391  O   LEU A 187     1117   1213   1311     29    -41    -57       O  
ATOM   1392  CB  LEU A 187      39.586  49.104  59.793  1.00 10.07           C  
ANISOU 1392  CB  LEU A 187     1201   1267   1359     18    -44    -61       C  
ATOM   1393  CG  LEU A 187      39.597  50.648  59.883  1.00 10.85           C  
ANISOU 1393  CG  LEU A 187     1311   1363   1449     11    -47    -63       C  
ATOM   1394  CD1 LEU A 187      38.438  51.080  60.772  1.00 11.75           C  
ANISOU 1394  CD1 LEU A 187     1435   1471   1559     18    -47    -61       C  
ATOM   1395  CD2 LEU A 187      40.889  51.177  60.399  1.00 12.54           C  
ANISOU 1395  CD2 LEU A 187     1523   1583   1658      2    -51    -66       C  
ATOM   1396  N   ALA A 188      40.803  46.382  57.824  1.00  8.44           N  
ANISOU 1396  N   ALA A 188      970   1066   1171     21    -36    -64       N  
ATOM   1397  CA  ALA A 188      40.799  44.955  57.877  1.00  9.08           C  
ANISOU 1397  CA  ALA A 188     1044   1144   1260     29    -32    -63       C  
ATOM   1398  C   ALA A 188      42.078  44.392  58.500  1.00  9.50           C  
ANISOU 1398  C   ALA A 188     1087   1205   1316     34    -33    -61       C  
ATOM   1399  O   ALA A 188      43.141  45.022  58.393  1.00 10.11           O  
ANISOU 1399  O   ALA A 188     1161   1292   1390     28    -35    -62       O  
ATOM   1400  CB  ALA A 188      40.644  44.410  56.515  1.00  9.02           C  
ANISOU 1400  CB  ALA A 188     1035   1134   1257     27    -28    -69       C  
ATOM   1401  N   ARG A 189      41.953  43.224  59.154  1.00  9.32           N  
ANISOU 1401  N   ARG A 189     1060   1179   1301     44    -31    -55       N  
ATOM   1402  CA AARG A 189      43.082  42.542  59.766  0.60 10.02           C  
ANISOU 1402  CA AARG A 189     1139   1276   1393     50    -31    -51       C  
ATOM   1403  CA BARG A 189      43.073  42.554  59.800  0.40 10.08           C  
ANISOU 1403  CA BARG A 189     1147   1283   1401     50    -31    -51       C  
ATOM   1404  C   ARG A 189      42.883  41.059  59.662  1.00  9.62           C  
ANISOU 1404  C   ARG A 189     1085   1216   1354     61    -25    -49       C  
ATOM   1405  O   ARG A 189      41.880  40.610  59.137  1.00 10.19           O  
ANISOU 1405  O   ARG A 189     1163   1278   1431     60    -22    -51       O  
ATOM   1406  CB AARG A 189      43.224  42.940  61.205  0.60 11.37           C  
ANISOU 1406  CB AARG A 189     1310   1453   1558     53    -37    -44       C  
ATOM   1407  CB BARG A 189      43.155  42.945  61.269  0.40 11.34           C  
ANISOU 1407  CB BARG A 189     1306   1449   1554     53    -37    -44       C  
ATOM   1408  CG AARG A 189      43.749  44.336  61.387  0.60 12.68           C  
ANISOU 1408  CG AARG A 189     1478   1627   1713     42    -43    -48       C  
ATOM   1409  CG BARG A 189      43.417  44.422  61.486  0.40 12.47           C  
ANISOU 1409  CG BARG A 189     1454   1598   1685     42    -43    -47       C  
ATOM   1410  CD AARG A 189      44.055  44.616  62.833  0.60 13.60           C  
ANISOU 1410  CD AARG A 189     1594   1752   1822     44    -50    -42       C  
ATOM   1411  CD BARG A 189      43.751  44.782  62.923  0.40 13.35           C  
ANISOU 1411  CD BARG A 189     1566   1719   1790     44    -50    -42       C  
ATOM   1412  NE AARG A 189      44.409  46.001  63.092  0.60 13.66           N  
ANISOU 1412  NE AARG A 189     1606   1765   1819     33    -56    -47       N  
ATOM   1413  NE BARG A 189      44.993  44.172  63.446  0.40 14.32           N  
ANISOU 1413  NE BARG A 189     1675   1853   1913     48    -53    -38       N  
ATOM   1414  CZ AARG A 189      45.625  46.517  63.001  0.60 14.87           C  
ANISOU 1414  CZ AARG A 189     1752   1929   1968     24    -60    -49       C  
ATOM   1415  CZ BARG A 189      46.175  44.786  63.489  0.40 14.40           C  
ANISOU 1415  CZ BARG A 189     1677   1875   1918     41    -58    -40       C  
ATOM   1416  NH1AARG A 189      45.795  47.820  63.308  0.60 15.97           N  
ANISOU 1416  NH1AARG A 189     1899   2072   2098     12    -66    -54       N  
ATOM   1417  NH1BARG A 189      47.239  44.183  64.021  0.40 14.93           N  
ANISOU 1417  NH1BARG A 189     1731   1955   1986     47    -60    -34       N  
ATOM   1418  NH2AARG A 189      46.674  45.756  62.642  0.60 15.20           N  
ANISOU 1418  NH2AARG A 189     1779   1979   2016     28    -58    -47       N  
ATOM   1419  NH2BARG A 189      46.305  46.009  62.998  0.40 15.24           N  
ANISOU 1419  NH2BARG A 189     1789   1983   2018     27    -60    -47       N  
ATOM   1420  N   ILE A 190      43.843  40.280  60.126  1.00  9.61           N  
ANISOU 1420  N   ILE A 190     1075   1220   1358     69    -24    -44       N  
ATOM   1421  CA  ILE A 190      43.717  38.846  60.193  1.00  9.64           C  
ANISOU 1421  CA  ILE A 190     1075   1213   1372     80    -18    -40       C  
ATOM   1422  C   ILE A 190      43.269  38.407  61.574  1.00 10.09           C  
ANISOU 1422  C   ILE A 190     1133   1269   1431     88    -21    -28       C  
ATOM   1423  O   ILE A 190      43.695  38.983  62.609  1.00  9.62           O  
ANISOU 1423  O   ILE A 190     1072   1222   1364     89    -27    -22       O  
ATOM   1424  CB  ILE A 190      45.060  38.164  59.844  1.00  9.84           C  
ANISOU 1424  CB  ILE A 190     1090   1245   1404     88    -14    -40       C  
ATOM   1425  CG1 ILE A 190      45.588  38.665  58.479  1.00 10.51           C  
ANISOU 1425  CG1 ILE A 190     1173   1334   1485     81    -11    -51       C  
ATOM   1426  CG2 ILE A 190      44.977  36.651  59.907  1.00 10.35           C  
ANISOU 1426  CG2 ILE A 190     1154   1297   1482    101     -7    -36       C  
ATOM   1427  CD1 ILE A 190      44.628  38.503  57.308  1.00 10.32           C  
ANISOU 1427  CD1 ILE A 190     1159   1298   1464     75     -6    -61       C  
ATOM   1428  N   ALA A 191      42.462  37.347  61.619  1.00  9.82           N  
ANISOU 1428  N   ALA A 191     1103   1221   1406     94    -16    -25       N  
ATOM   1429  CA  ALA A 191      42.027  36.758  62.882  1.00 10.11           C  
ANISOU 1429  CA  ALA A 191     1140   1255   1445    102    -16    -12       C  
ATOM   1430  C   ALA A 191      43.261  36.426  63.700  1.00 10.41           C  
ANISOU 1430  C   ALA A 191     1168   1303   1483    112    -18     -3       C  
ATOM   1431  O   ALA A 191      44.207  35.838  63.207  1.00 11.02           O  
ANISOU 1431  O   ALA A 191     1239   1382   1567    118    -15     -5       O  
ATOM   1432  CB  ALA A 191      41.176  35.525  62.651  1.00 10.27           C  
ANISOU 1432  CB  ALA A 191     1166   1258   1480    106     -9    -10       C  
ATOM   1433  N   ASP A 192      43.266  36.867  64.961  1.00 10.71           N  
ANISOU 1433  N   ASP A 192     1205   1352   1512    114    -24      6       N  
ATOM   1434  CA  ASP A 192      44.470  36.722  65.817  1.00 12.06           C  
ANISOU 1434  CA  ASP A 192     1366   1538   1679    123    -29     15       C  
ATOM   1435  C   ASP A 192      43.949  36.583  67.269  1.00 11.70           C  
ANISOU 1435  C   ASP A 192     1323   1495   1627    129    -32     28       C  
ATOM   1436  O   ASP A 192      44.187  37.489  68.107  1.00 11.30           O  
ANISOU 1436  O   ASP A 192     1272   1460   1563    125    -40     29       O  
ATOM   1437  CB  ASP A 192      45.350  37.942  65.658  1.00 13.76           C  
ANISOU 1437  CB  ASP A 192     1576   1769   1882    113    -36      7       C  
ATOM   1438  CG  ASP A 192      46.752  37.733  66.169  1.00 16.31           C  
ANISOU 1438  CG  ASP A 192     1886   2109   2204    121    -40     14       C  
ATOM   1439  OD1 ASP A 192      47.050  36.643  66.700  1.00 17.59           O  
ANISOU 1439  OD1 ASP A 192     2042   2270   2373    135    -38     26       O  
ATOM   1440  OD2 ASP A 192      47.545  38.715  66.019  1.00 17.94           O  
ANISOU 1440  OD2 ASP A 192     2086   2329   2401    111    -46      9       O  
ATOM   1441  N   PRO A 193      43.318  35.436  67.550  1.00 12.93           N  
ANISOU 1441  N   PRO A 193     1482   1638   1794    137    -26     37       N  
ATOM   1442  CA  PRO A 193      42.751  35.220  68.905  1.00 13.04           C  
ANISOU 1442  CA  PRO A 193     1498   1654   1802    143    -27     51       C  
ATOM   1443  C   PRO A 193      43.825  35.320  69.995  1.00 13.64           C  
ANISOU 1443  C   PRO A 193     1565   1749   1868    151    -35     61       C  
ATOM   1444  O   PRO A 193      43.525  35.793  71.101  1.00 12.56           O  
ANISOU 1444  O   PRO A 193     1432   1624   1719    151    -40     68       O  
ATOM   1445  CB  PRO A 193      42.180  33.783  68.813  1.00 13.82           C  
ANISOU 1445  CB  PRO A 193     1599   1734   1917    152    -18     60       C  
ATOM   1446  CG  PRO A 193      42.876  33.146  67.660  1.00 15.29           C  
ANISOU 1446  CG  PRO A 193     1782   1912   2117    154    -13     53       C  
ATOM   1447  CD  PRO A 193      43.050  34.275  66.675  1.00 14.26           C  
ANISOU 1447  CD  PRO A 193     1652   1787   1979    142    -16     36       C  
ATOM   1448  N   GLU A 194      45.071  34.962  69.692  1.00 12.08           N  
ANISOU 1448  N   GLU A 194     1356   1558   1674    157    -36     62       N  
ATOM   1449  CA AGLU A 194      46.119  35.052  70.705  0.50 12.72           C  
ANISOU 1449  CA AGLU A 194     1427   1660   1746    165    -44     73       C  
ATOM   1450  CA BGLU A 194      46.134  35.082  70.680  0.50 12.90           C  
ANISOU 1450  CA BGLU A 194     1450   1683   1768    164    -44     72       C  
ATOM   1451  C   GLU A 194      46.228  36.462  71.263  1.00 12.65           C  
ANISOU 1451  C   GLU A 194     1421   1669   1718    152    -54     66       C  
ATOM   1452  O   GLU A 194      46.504  36.620  72.486  1.00 13.84           O  
ANISOU 1452  O   GLU A 194     1568   1835   1856    156    -62     76       O  
ATOM   1453  CB AGLU A 194      47.517  34.587  70.183  0.50 12.41           C  
ANISOU 1453  CB AGLU A 194     1374   1628   1714    172    -44     74       C  
ATOM   1454  CB BGLU A 194      47.495  34.789  70.061  0.50 12.86           C  
ANISOU 1454  CB BGLU A 194     1431   1686   1770    170    -44     71       C  
ATOM   1455  CG AGLU A 194      48.699  35.053  71.066  0.50 12.94           C  
ANISOU 1455  CG AGLU A 194     1427   1722   1768    175    -55     81       C  
ATOM   1456  CG BGLU A 194      47.739  33.362  69.776  0.50 13.49           C  
ANISOU 1456  CG BGLU A 194     1507   1752   1866    186    -35     80       C  
ATOM   1457  CD AGLU A 194      50.024  34.507  70.657  0.50 12.80           C  
ANISOU 1457  CD AGLU A 194     1393   1712   1757    185    -54     85       C  
ATOM   1458  CD BGLU A 194      48.952  33.174  68.941  0.50 13.71           C  
ANISOU 1458  CD BGLU A 194     1522   1785   1900    190    -33     76       C  
ATOM   1459  OE1AGLU A 194      50.155  34.097  69.498  0.50 13.39           O  
ANISOU 1459  OE1AGLU A 194     1467   1775   1845    186    -45     77       O  
ATOM   1460  OE1BGLU A 194      50.077  33.373  69.460  0.50 14.36           O  
ANISOU 1460  OE1BGLU A 194     1590   1889   1976    195    -40     82       O  
ATOM   1461  OE2AGLU A 194      50.940  34.530  71.493  0.50 11.87           O  
ANISOU 1461  OE2AGLU A 194     1263   1616   1632    191    -62     95       O  
ATOM   1462  OE2BGLU A 194      48.735  32.767  67.798  0.50 13.11           O  
ANISOU 1462  OE2BGLU A 194     1451   1694   1837    190    -24     66       O  
ATOM   1463  N   HIS A 195      45.999  37.479  70.417  1.00 12.14           N  
ANISOU 1463  N   HIS A 195     1362   1602   1651    138    -55     50       N  
ATOM   1464  CA  HIS A 195      46.238  38.873  70.776  1.00 13.50           C  
ANISOU 1464  CA  HIS A 195     1535   1788   1806    125    -65     42       C  
ATOM   1465  C   HIS A 195      44.979  39.738  70.900  1.00 12.89           C  
ANISOU 1465  C   HIS A 195     1473   1703   1721    116    -64     34       C  
ATOM   1466  O   HIS A 195      45.076  40.988  70.850  1.00 12.94           O  
ANISOU 1466  O   HIS A 195     1485   1715   1716    104    -70     23       O  
ATOM   1467  CB  HIS A 195      47.185  39.467  69.751  1.00 14.58           C  
ANISOU 1467  CB  HIS A 195     1666   1931   1945    116    -67     30       C  
ATOM   1468  CG  HIS A 195      48.537  38.834  69.778  1.00 15.90           C  
ANISOU 1468  CG  HIS A 195     1815   2110   2116    124    -69     38       C  
ATOM   1469  ND1 HIS A 195      49.050  38.094  68.738  1.00 17.25           N  
ANISOU 1469  ND1 HIS A 195     1978   2275   2301    130    -61     36       N  
ATOM   1470  CD2 HIS A 195      49.425  38.712  70.798  1.00 19.04           C  
ANISOU 1470  CD2 HIS A 195     2202   2528   2506    130    -77     48       C  
ATOM   1471  CE1 HIS A 195      50.259  37.665  69.071  1.00 17.11           C  
ANISOU 1471  CE1 HIS A 195     1944   2272   2283    139    -65     45       C  
ATOM   1472  NE2 HIS A 195      50.500  38.018  70.314  1.00 19.46           N  
ANISOU 1472  NE2 HIS A 195     2239   2587   2568    139    -75     53       N  
ATOM   1473  N   ASP A 196      43.835  39.080  71.083  1.00 12.33           N  
ANISOU 1473  N   ASP A 196     1410   1619   1656    123    -57     40       N  
ATOM   1474  CA  ASP A 196      42.548  39.818  71.120  1.00 12.01           C  
ANISOU 1474  CA  ASP A 196     1383   1571   1610    116    -54     34       C  
ATOM   1475  C   ASP A 196      42.397  40.698  72.358  1.00 12.19           C  
ANISOU 1475  C   ASP A 196     1411   1606   1614    114    -61     35       C  
ATOM   1476  O   ASP A 196      41.654  41.688  72.341  1.00 12.07           O  
ANISOU 1476  O   ASP A 196     1407   1588   1591    107    -61     27       O  
ATOM   1477  CB  ASP A 196      41.374  38.881  71.021  1.00 12.04           C  
ANISOU 1477  CB  ASP A 196     1390   1559   1625    122    -45     42       C  
ATOM   1478  CG  ASP A 196      40.067  39.612  70.765  1.00 13.14           C  
ANISOU 1478  CG  ASP A 196     1541   1690   1762    115    -42     35       C  
ATOM   1479  OD1 ASP A 196      39.920  40.208  69.672  1.00 14.41           O  
ANISOU 1479  OD1 ASP A 196     1705   1846   1926    106    -41     23       O  
ATOM   1480  OD2 ASP A 196      39.173  39.565  71.617  1.00 12.80           O  
ANISOU 1480  OD2 ASP A 196     1503   1647   1714    119    -39     42       O  
ATOM   1481  N   HIS A 197      43.033  40.302  73.462  1.00 13.16           N  
ANISOU 1481  N   HIS A 197     1529   1743   1730    122    -66     46       N  
ATOM   1482  CA  HIS A 197      42.733  40.963  74.766  1.00 12.36           C  
ANISOU 1482  CA  HIS A 197     1434   1654   1609    122    -71     48       C  
ATOM   1483  C   HIS A 197      43.265  42.379  74.869  1.00 11.83           C  
ANISOU 1483  C   HIS A 197     1372   1597   1527    109    -80     34       C  
ATOM   1484  O   HIS A 197      44.379  42.679  74.421  1.00 13.20           O  
ANISOU 1484  O   HIS A 197     1537   1778   1701    102    -87     29       O  
ATOM   1485  CB  HIS A 197      43.309  40.177  75.909  1.00 13.05           C  
ANISOU 1485  CB  HIS A 197     1514   1755   1690    133    -75     64       C  
ATOM   1486  CG  HIS A 197      42.863  40.709  77.234  1.00 13.63           C  
ANISOU 1486  CG  HIS A 197     1596   1840   1743    134    -78     67       C  
ATOM   1487  ND1 HIS A 197      43.640  41.513  78.013  1.00 14.26           N  
ANISOU 1487  ND1 HIS A 197     1675   1938   1804    129    -90     62       N  
ATOM   1488  CD2 HIS A 197      41.659  40.620  77.840  1.00 13.66           C  
ANISOU 1488  CD2 HIS A 197     1609   1839   1743    139    -71     73       C  
ATOM   1489  CE1 HIS A 197      42.923  41.902  79.072  1.00 14.76           C  
ANISOU 1489  CE1 HIS A 197     1750   2008   1852    131    -89     64       C  
ATOM   1490  NE2 HIS A 197      41.732  41.358  78.981  1.00 14.08           N  
ANISOU 1490  NE2 HIS A 197     1669   1908   1774    138    -78     71       N  
ATOM   1491  N   THR A 198      42.479  43.270  75.467  1.00 11.08           N  
ANISOU 1491  N   THR A 198     1290   1502   1418    106    -80     29       N  
ATOM   1492  CA  THR A 198      42.942  44.582  75.783  1.00 10.69           C  
ANISOU 1492  CA  THR A 198     1247   1461   1353     94    -89     16       C  
ATOM   1493  C   THR A 198      42.165  45.092  77.010  1.00 10.94           C  
ANISOU 1493  C   THR A 198     1291   1497   1367     97    -88     16       C  
ATOM   1494  O   THR A 198      41.282  44.436  77.509  1.00 10.67           O  
ANISOU 1494  O   THR A 198     1259   1460   1333    108    -81     27       O  
ATOM   1495  CB  THR A 198      42.770  45.536  74.559  1.00 11.44           C  
ANISOU 1495  CB  THR A 198     1349   1544   1455     82    -87      1       C  
ATOM   1496  OG1 THR A 198      43.399  46.776  74.825  1.00 12.49           O  
ANISOU 1496  OG1 THR A 198     1488   1684   1575     69    -95    -11       O  
ATOM   1497  CG2 THR A 198      41.301  45.781  74.274  1.00 11.89           C  
ANISOU 1497  CG2 THR A 198     1417   1584   1515     85    -77     -1       C  
ATOM   1498  N   GLY A 199      42.498  46.259  77.509  1.00 10.54           N  
ANISOU 1498  N   GLY A 199     1250   1455   1300     88    -96      4       N  
ATOM   1499  CA  GLY A 199      41.853  46.829  78.673  1.00 11.26           C  
ANISOU 1499  CA  GLY A 199     1355   1552   1372     91    -96      2       C  
ATOM   1500  C   GLY A 199      40.492  47.437  78.397  1.00 12.15           C  
ANISOU 1500  C   GLY A 199     1483   1649   1487     93    -85     -4       C  
ATOM   1501  O   GLY A 199      40.087  47.620  77.266  1.00 13.55           O  
ANISOU 1501  O   GLY A 199     1660   1811   1678     90    -80     -9       O  
ATOM   1502  N   PHE A 200      39.837  47.872  79.466  1.00 11.92           N  
ANISOU 1502  N   PHE A 200     1464   1624   1440     98    -83     -5       N  
ATOM   1503  CA  PHE A 200      38.569  48.551  79.426  1.00 12.21           C  
ANISOU 1503  CA  PHE A 200     1516   1649   1475    102    -73    -11       C  
ATOM   1504  C   PHE A 200      38.750  49.914  78.782  1.00 12.97           C  
ANISOU 1504  C   PHE A 200     1624   1736   1570     89    -76    -29       C  
ATOM   1505  O   PHE A 200      39.703  50.631  79.071  1.00 13.41           O  
ANISOU 1505  O   PHE A 200     1684   1798   1614     78    -86    -40       O  
ATOM   1506  CB  PHE A 200      38.103  48.666  80.869  1.00 11.65           C  
ANISOU 1506  CB  PHE A 200     1454   1590   1383    111    -71     -8       C  
ATOM   1507  CG  PHE A 200      36.790  49.381  81.095  1.00 12.00           C  
ANISOU 1507  CG  PHE A 200     1513   1625   1421    117    -60    -13       C  
ATOM   1508  CD1 PHE A 200      35.624  48.968  80.482  1.00 11.88           C  
ANISOU 1508  CD1 PHE A 200     1495   1598   1421    125    -48     -6       C  
ATOM   1509  CD2 PHE A 200      36.729  50.391  82.044  1.00 12.06           C  
ANISOU 1509  CD2 PHE A 200     1537   1638   1406    117    -62    -25       C  
ATOM   1510  CE1 PHE A 200      34.436  49.588  80.752  1.00 11.94           C  
ANISOU 1510  CE1 PHE A 200     1515   1601   1423    133    -38     -9       C  
ATOM   1511  CE2 PHE A 200      35.520  50.983  82.333  1.00 12.32           C  
ANISOU 1511  CE2 PHE A 200     1583   1665   1433    125    -50    -29       C  
ATOM   1512  CZ  PHE A 200      34.398  50.581  81.681  1.00 12.04           C  
ANISOU 1512  CZ  PHE A 200     1543   1618   1414    134    -39    -20       C  
ATOM   1513  N   LEU A 201      37.749  50.261  77.971  1.00 13.41           N  
ANISOU 1513  N   LEU A 201     1685   1774   1636     92    -67    -32       N  
ATOM   1514  CA  LEU A 201      37.699  51.558  77.264  1.00 15.66           C  
ANISOU 1514  CA  LEU A 201     1983   2047   1921     82    -67    -47       C  
ATOM   1515  C   LEU A 201      38.954  51.840  76.413  1.00 16.28           C  
ANISOU 1515  C   LEU A 201     2055   2124   2006     67    -77    -54       C  
ATOM   1516  O   LEU A 201      39.458  52.960  76.395  1.00 19.54           O  
ANISOU 1516  O   LEU A 201     2479   2534   2411     55    -82    -68       O  
ATOM   1517  CB  LEU A 201      37.465  52.735  78.244  1.00 18.52           C  
ANISOU 1517  CB  LEU A 201     2365   2410   2263     82    -67    -60       C  
ATOM   1518  CG  LEU A 201      36.257  52.591  79.192  1.00 19.81           C  
ANISOU 1518  CG  LEU A 201     2535   2575   2416     98    -57    -54       C  
ATOM   1519  CD1 LEU A 201      36.172  53.793  80.125  1.00 23.53           C  
ANISOU 1519  CD1 LEU A 201     3027   3047   2866     97    -58    -68       C  
ATOM   1520  CD2 LEU A 201      34.971  52.376  78.455  1.00 19.93           C  
ANISOU 1520  CD2 LEU A 201     2548   2578   2445    108    -45    -47       C  
ATOM   1521  N   THR A 202      39.419  50.846  75.674  1.00 15.05           N  
ANISOU 1521  N   THR A 202     1882   1970   1865     66    -78    -46       N  
ATOM   1522  CA  THR A 202      40.517  51.003  74.694  1.00 15.21           C  
ANISOU 1522  CA  THR A 202     1895   1990   1895     53    -84    -51       C  
ATOM   1523  C   THR A 202      39.990  51.717  73.465  1.00 15.73           C  
ANISOU 1523  C   THR A 202     1968   2039   1971     48    -79    -57       C  
ATOM   1524  O   THR A 202      38.942  51.341  72.920  1.00 15.01           O  
ANISOU 1524  O   THR A 202     1876   1938   1889     57    -70    -52       O  
ATOM   1525  CB  THR A 202      41.097  49.627  74.263  1.00 14.75           C  
ANISOU 1525  CB  THR A 202     1817   1938   1849     57    -85    -39       C  
ATOM   1526  OG1 THR A 202      41.685  48.944  75.424  1.00 16.18           O  
ANISOU 1526  OG1 THR A 202     1990   2136   2021     63    -91    -30       O  
ATOM   1527  CG2 THR A 202      42.221  49.787  73.210  1.00 15.68           C  
ANISOU 1527  CG2 THR A 202     1926   2057   1977     45    -90    -44       C  
ATOM   1528  N   GLU A 203      40.715  52.740  73.018  1.00 15.97           N  
ANISOU 1528  N   GLU A 203     2004   2066   1999     34    -84    -68       N  
ATOM   1529  CA  GLU A 203      40.298  53.500  71.835  1.00 17.30           C  
ANISOU 1529  CA  GLU A 203     2180   2218   2176     28    -79    -74       C  
ATOM   1530  C   GLU A 203      40.199  52.564  70.624  1.00 16.29           C  
ANISOU 1530  C   GLU A 203     2038   2087   2065     31    -75    -66       C  
ATOM   1531  O   GLU A 203      40.946  51.596  70.485  1.00 16.13           O  
ANISOU 1531  O   GLU A 203     2002   2076   2050     31    -78    -60       O  
ATOM   1532  CB  GLU A 203      41.272  54.659  71.593  1.00 21.76           C  
ANISOU 1532  CB  GLU A 203     2752   2781   2735     10    -86    -86       C  
ATOM   1533  CG  GLU A 203      41.419  55.499  72.840  1.00 28.35           C  
ANISOU 1533  CG  GLU A 203     3601   3619   3553      6    -92    -95       C  
ATOM   1534  CD  GLU A 203      41.501  56.981  72.587  1.00 36.32           C  
ANISOU 1534  CD  GLU A 203     4628   4614   4556     -6    -92   -108       C  
ATOM   1535  OE1 GLU A 203      42.504  57.397  71.936  1.00 44.33           O  
ANISOU 1535  OE1 GLU A 203     5639   5629   5575    -23    -98   -112       O  
ATOM   1536  OE2 GLU A 203      40.607  57.726  73.104  1.00 40.56           O  
ANISOU 1536  OE2 GLU A 203     5184   5141   5086      0    -87   -113       O  
ATOM   1537  N   TYR A 204      39.246  52.845  69.745  1.00 16.41           N  
ANISOU 1537  N   TYR A 204     2059   2089   2087     34    -67    -66       N  
ATOM   1538  CA  TYR A 204      38.962  51.959  68.618  1.00 16.26           C  
ANISOU 1538  CA  TYR A 204     2028   2067   2083     38    -63    -60       C  
ATOM   1539  C   TYR A 204      38.656  52.806  67.422  1.00 17.92           C  
ANISOU 1539  C   TYR A 204     2246   2266   2298     31    -60    -65       C  
ATOM   1540  O   TYR A 204      38.066  53.869  67.557  1.00 20.83           O  
ANISOU 1540  O   TYR A 204     2628   2625   2660     32    -58    -69       O  
ATOM   1541  CB  TYR A 204      37.742  51.036  68.938  1.00 15.79           C  
ANISOU 1541  CB  TYR A 204     1965   2006   2027     52    -56    -50       C  
ATOM   1542  CG  TYR A 204      37.644  49.803  68.108  1.00 14.68           C  
ANISOU 1542  CG  TYR A 204     1812   1865   1901     55    -53    -44       C  
ATOM   1543  CD1 TYR A 204      38.589  48.785  68.212  1.00 14.83           C  
ANISOU 1543  CD1 TYR A 204     1818   1892   1925     55    -56    -39       C  
ATOM   1544  CD2 TYR A 204      36.559  49.584  67.241  1.00 13.79           C  
ANISOU 1544  CD2 TYR A 204     1699   1744   1797     59    -47    -41       C  
ATOM   1545  CE1 TYR A 204      38.512  47.686  67.429  1.00 15.25           C  
ANISOU 1545  CE1 TYR A 204     1861   1943   1991     58    -52    -34       C  
ATOM   1546  CE2 TYR A 204      36.501  48.450  66.472  1.00 13.56           C  
ANISOU 1546  CE2 TYR A 204     1659   1714   1781     60    -44    -36       C  
ATOM   1547  CZ  TYR A 204      37.474  47.497  66.593  1.00 14.89           C  
ANISOU 1547  CZ  TYR A 204     1817   1889   1953     60    -47    -34       C  
ATOM   1548  OH  TYR A 204      37.387  46.326  65.823  1.00 18.19           O  
ANISOU 1548  OH  TYR A 204     2225   2303   2384     62    -43    -30       O  
ATOM   1549  N   VAL A 205      39.073  52.341  66.243  1.00 19.75           N  
ANISOU 1549  N   VAL A 205     2467   2496   2539     27    -60    -63       N  
ATOM   1550  CA  VAL A 205      38.993  53.201  65.077  1.00 21.63           C  
ANISOU 1550  CA  VAL A 205     2712   2726   2780     19    -58    -67       C  
ATOM   1551  C   VAL A 205      37.695  52.992  64.280  1.00 18.35           C  
ANISOU 1551  C   VAL A 205     2298   2303   2372     27    -51    -63       C  
ATOM   1552  O   VAL A 205      37.244  53.895  63.647  1.00 23.24           O  
ANISOU 1552  O   VAL A 205     2926   2913   2990     25    -49    -65       O  
ATOM   1553  CB  VAL A 205      40.130  52.932  64.078  1.00 23.68           C  
ANISOU 1553  CB  VAL A 205     2961   2991   3046      8    -60    -69       C  
ATOM   1554  CG1 VAL A 205      40.060  53.949  62.945  1.00 25.28           C  
ANISOU 1554  CG1 VAL A 205     3171   3184   3249      0    -58    -72       C  
ATOM   1555  CG2 VAL A 205      41.494  52.992  64.758  1.00 24.69           C  
ANISOU 1555  CG2 VAL A 205     3083   3130   3169      0    -67    -72       C  
ATOM   1556  N   ALA A 206      37.134  51.796  64.316  1.00 15.22           N  
ANISOU 1556  N   ALA A 206     1891   1909   1982     36    -48    -57       N  
ATOM   1557  CA  ALA A 206      35.917  51.513  63.515  1.00 14.32           C  
ANISOU 1557  CA  ALA A 206     1777   1790   1875     42    -43    -52       C  
ATOM   1558  C   ALA A 206      34.696  52.280  64.012  1.00 13.21           C  
ANISOU 1558  C   ALA A 206     1646   1643   1729     50    -40    -51       C  
ATOM   1559  O   ALA A 206      34.585  52.735  65.151  1.00 13.09           O  
ANISOU 1559  O   ALA A 206     1639   1629   1705     55    -39    -52       O  
ATOM   1560  CB  ALA A 206      35.667  50.042  63.488  1.00 15.26           C  
ANISOU 1560  CB  ALA A 206     1883   1913   2002     47    -41    -47       C  
ATOM   1561  N   THR A 207      33.723  52.393  63.120  1.00 12.23           N  
ANISOU 1561  N   THR A 207     1523   1515   1609     53    -36    -48       N  
ATOM   1562  CA  THR A 207      32.534  53.157  63.339  1.00 11.56           C  
ANISOU 1562  CA  THR A 207     1446   1425   1521     62    -32    -45       C  
ATOM   1563  C   THR A 207      31.779  52.785  64.624  1.00 11.46           C  
ANISOU 1563  C   THR A 207     1433   1415   1505     73    -28    -40       C  
ATOM   1564  O   THR A 207      31.382  51.649  64.823  1.00 11.57           O  
ANISOU 1564  O   THR A 207     1436   1434   1524     77    -27    -34       O  
ATOM   1565  CB  THR A 207      31.627  52.977  62.139  1.00 11.13           C  
ANISOU 1565  CB  THR A 207     1387   1369   1473     64    -30    -40       C  
ATOM   1566  OG1 THR A 207      32.400  53.216  60.930  1.00 11.30           O  
ANISOU 1566  OG1 THR A 207     1407   1389   1496     53    -33    -44       O  
ATOM   1567  CG2 THR A 207      30.469  53.884  62.205  1.00 10.99           C  
ANISOU 1567  CG2 THR A 207     1377   1347   1452     73    -26    -37       C  
ATOM   1568  N   ARG A 208      31.519  53.799  65.464  1.00 10.36           N  
ANISOU 1568  N   ARG A 208     1306   1272   1356     79    -26    -43       N  
ATOM   1569  CA  ARG A 208      31.002  53.568  66.794  1.00 10.41           C  
ANISOU 1569  CA  ARG A 208     1315   1284   1357     89    -22    -40       C  
ATOM   1570  C   ARG A 208      29.743  52.688  66.856  1.00 10.00           C  
ANISOU 1570  C   ARG A 208     1252   1236   1311     99    -17    -29       C  
ATOM   1571  O   ARG A 208      29.661  51.762  67.626  1.00  9.38           O  
ANISOU 1571  O   ARG A 208     1166   1164   1233    102    -15    -24       O  
ATOM   1572  CB  ARG A 208      30.719  54.938  67.429  1.00 12.36           C  
ANISOU 1572  CB  ARG A 208     1580   1524   1594     95    -19    -46       C  
ATOM   1573  CG  ARG A 208      30.383  54.799  68.881  1.00 12.79           C  
ANISOU 1573  CG  ARG A 208     1638   1585   1639    104    -16    -44       C  
ATOM   1574  CD  ARG A 208      29.862  56.089  69.509  1.00 14.22           C  
ANISOU 1574  CD  ARG A 208     1837   1758   1809    113    -10    -50       C  
ATOM   1575  NE  ARG A 208      30.811  57.172  69.373  1.00 15.14           N  
ANISOU 1575  NE  ARG A 208     1967   1865   1920    102    -15    -61       N  
ATOM   1576  CZ  ARG A 208      30.503  58.360  68.904  1.00 18.21           C  
ANISOU 1576  CZ  ARG A 208     2370   2241   2308    104    -12    -66       C  
ATOM   1577  NH1 ARG A 208      29.246  58.691  68.553  1.00 20.20           N  
ANISOU 1577  NH1 ARG A 208     2623   2488   2563    118     -5    -59       N  
ATOM   1578  NH2 ARG A 208      31.487  59.276  68.811  1.00 19.79           N  
ANISOU 1578  NH2 ARG A 208     2583   2432   2504     91    -18    -76       N  
ATOM   1579  N   TRP A 209      28.737  53.015  66.049  1.00  9.08           N  
ANISOU 1579  N   TRP A 209     1134   1117   1200    103    -13    -26       N  
ATOM   1580  CA  TRP A 209      27.427  52.399  66.187  1.00  9.40           C  
ANISOU 1580  CA  TRP A 209     1165   1163   1245    113     -8    -16       C  
ATOM   1581  C   TRP A 209      27.410  50.906  65.892  1.00  8.53           C  
ANISOU 1581  C   TRP A 209     1039   1058   1145    108     -9    -10       C  
ATOM   1582  O   TRP A 209      26.462  50.239  66.220  1.00  8.61           O  
ANISOU 1582  O   TRP A 209     1040   1072   1159    113     -5     -1       O  
ATOM   1583  CB  TRP A 209      26.426  53.054  65.273  1.00  9.89           C  
ANISOU 1583  CB  TRP A 209     1227   1221   1310    118     -5    -12       C  
ATOM   1584  CG  TRP A 209      26.186  54.516  65.560  1.00 10.45           C  
ANISOU 1584  CG  TRP A 209     1313   1284   1372    126     -1    -16       C  
ATOM   1585  CD1 TRP A 209      26.528  55.232  66.681  1.00 11.00           C  
ANISOU 1585  CD1 TRP A 209     1398   1351   1432    131      1    -22       C  
ATOM   1586  CD2 TRP A 209      25.429  55.405  64.732  1.00 10.95           C  
ANISOU 1586  CD2 TRP A 209     1380   1343   1436    132      1    -13       C  
ATOM   1587  NE1 TRP A 209      26.062  56.518  66.573  1.00 11.36           N  
ANISOU 1587  NE1 TRP A 209     1456   1388   1472    139      5    -24       N  
ATOM   1588  CE2 TRP A 209      25.417  56.661  65.378  1.00 11.50           C  
ANISOU 1588  CE2 TRP A 209     1467   1404   1497    140      5    -18       C  
ATOM   1589  CE3 TRP A 209      24.883  55.303  63.451  1.00 11.16           C  
ANISOU 1589  CE3 TRP A 209     1398   1371   1470    130     -2     -8       C  
ATOM   1590  CZ2 TRP A 209      24.806  57.760  64.829  1.00 12.72           C  
ANISOU 1590  CZ2 TRP A 209     1631   1551   1652    148      8    -16       C  
ATOM   1591  CZ3 TRP A 209      24.257  56.417  62.900  1.00 12.48           C  
ANISOU 1591  CZ3 TRP A 209     1573   1533   1636    138      1     -5       C  
ATOM   1592  CH2 TRP A 209      24.227  57.617  63.575  1.00 12.09           C  
ANISOU 1592  CH2 TRP A 209     1540   1474   1579    148      6     -8       C  
ATOM   1593  N   TYR A 210      28.456  50.413  65.216  1.00  8.41           N  
ANISOU 1593  N   TYR A 210     1020   1040   1134     96    -15    -15       N  
ATOM   1594  CA  TYR A 210      28.531  49.006  64.779  1.00  8.56           C  
ANISOU 1594  CA  TYR A 210     1027   1062   1164     91    -16    -11       C  
ATOM   1595  C   TYR A 210      29.550  48.192  65.571  1.00  8.33           C  
ANISOU 1595  C   TYR A 210      996   1036   1135     89    -18    -11       C  
ATOM   1596  O   TYR A 210      29.785  47.084  65.227  1.00  8.19           O  
ANISOU 1596  O   TYR A 210      969   1017   1126     85    -19     -9       O  
ATOM   1597  CB  TYR A 210      28.780  48.934  63.270  1.00  8.76           C  
ANISOU 1597  CB  TYR A 210     1049   1084   1195     82    -20    -16       C  
ATOM   1598  CG  TYR A 210      27.712  49.755  62.534  1.00  8.43           C  
ANISOU 1598  CG  TYR A 210     1008   1041   1152     85    -19    -13       C  
ATOM   1599  CD1 TYR A 210      26.482  49.207  62.199  1.00  8.93           C  
ANISOU 1599  CD1 TYR A 210     1062   1109   1222     88    -17     -6       C  
ATOM   1600  CD2 TYR A 210      27.893  51.104  62.272  1.00  8.65           C  
ANISOU 1600  CD2 TYR A 210     1048   1066   1174     86    -20    -17       C  
ATOM   1601  CE1 TYR A 210      25.482  49.987  61.653  1.00  8.78           C  
ANISOU 1601  CE1 TYR A 210     1043   1091   1201     93    -16     -2       C  
ATOM   1602  CE2 TYR A 210      26.891  51.883  61.764  1.00  8.70           C  
ANISOU 1602  CE2 TYR A 210     1057   1071   1179     92    -18    -14       C  
ATOM   1603  CZ  TYR A 210      25.694  51.334  61.434  1.00  8.63           C  
ANISOU 1603  CZ  TYR A 210     1037   1068   1176     96    -16     -6       C  
ATOM   1604  OH  TYR A 210      24.660  52.078  60.900  1.00  8.93           O  
ANISOU 1604  OH  TYR A 210     1074   1107   1212    103    -14      0       O  
ATOM   1605  N   ARG A 211      30.075  48.774  66.645  1.00  8.27           N  
ANISOU 1605  N   ARG A 211      996   1030   1117     93    -19    -13       N  
ATOM   1606  CA  ARG A 211      31.044  48.098  67.532  1.00  9.06           C  
ANISOU 1606  CA  ARG A 211     1094   1135   1215     92    -21    -12       C  
ATOM   1607  C   ARG A 211      30.392  47.136  68.476  1.00  8.85           C  
ANISOU 1607  C   ARG A 211     1061   1113   1189    100    -16     -2       C  
ATOM   1608  O   ARG A 211      29.489  47.537  69.218  1.00  8.85           O  
ANISOU 1608  O   ARG A 211     1065   1116   1183    108    -11      3       O  
ATOM   1609  CB  ARG A 211      31.759  49.153  68.384  1.00 10.48           C  
ANISOU 1609  CB  ARG A 211     1285   1317   1380     92    -24    -19       C  
ATOM   1610  CG  ARG A 211      32.657  50.162  67.689  1.00 11.39           C  
ANISOU 1610  CG  ARG A 211     1407   1427   1492     83    -29    -30       C  
ATOM   1611  CD  ARG A 211      33.197  51.240  68.653  1.00 11.96           C  
ANISOU 1611  CD  ARG A 211     1493   1502   1550     82    -32    -37       C  
ATOM   1612  NE  ARG A 211      33.947  52.232  67.881  1.00 12.87           N  
ANISOU 1612  NE  ARG A 211     1615   1611   1664     72    -36    -46       N  
ATOM   1613  CZ  ARG A 211      34.257  53.450  68.346  1.00 13.35           C  
ANISOU 1613  CZ  ARG A 211     1690   1668   1714     69    -38    -54       C  
ATOM   1614  NH1 ARG A 211      33.898  53.839  69.572  1.00 14.21           N  
ANISOU 1614  NH1 ARG A 211     1808   1779   1812     76    -36    -55       N  
ATOM   1615  NH2 ARG A 211      34.863  54.313  67.519  1.00 13.95           N  
ANISOU 1615  NH2 ARG A 211     1772   1738   1791     58    -41    -61       N  
ATOM   1616  N   ALA A 212      30.902  45.890  68.538  1.00  8.47           N  
ANISOU 1616  N   ALA A 212     1004   1065   1149     98    -17      3       N  
ATOM   1617  CA  ALA A 212      30.419  44.912  69.475  1.00  8.48           C  
ANISOU 1617  CA  ALA A 212      999   1070   1152    104    -12     15       C  
ATOM   1618  C   ALA A 212      30.701  45.361  70.892  1.00  8.71           C  
ANISOU 1618  C   ALA A 212     1035   1107   1166    111    -12     17       C  
ATOM   1619  O   ALA A 212      31.644  46.126  71.155  1.00  7.97           O  
ANISOU 1619  O   ALA A 212      949   1017   1063    109    -18      9       O  
ATOM   1620  CB  ALA A 212      31.096  43.609  69.233  1.00  9.22           C  
ANISOU 1620  CB  ALA A 212     1086   1162   1257    101    -14     19       C  
ATOM   1621  N   PRO A 213      29.936  44.844  71.852  1.00  8.73           N  
ANISOU 1621  N   PRO A 213     1036   1115   1167    119     -6     28       N  
ATOM   1622  CA  PRO A 213      30.126  45.341  73.235  1.00  8.96           C  
ANISOU 1622  CA  PRO A 213     1073   1154   1179    126     -5     30       C  
ATOM   1623  C   PRO A 213      31.534  45.079  73.776  1.00  8.61           C  
ANISOU 1623  C   PRO A 213     1028   1114   1128    124    -13     28       C  
ATOM   1624  O   PRO A 213      32.082  45.892  74.517  1.00  9.09           O  
ANISOU 1624  O   PRO A 213     1097   1182   1174    125    -17     22       O  
ATOM   1625  CB  PRO A 213      29.088  44.566  74.064  1.00  8.96           C  
ANISOU 1625  CB  PRO A 213     1067   1158   1180    135      3     44       C  
ATOM   1626  CG  PRO A 213      28.605  43.428  73.153  1.00  8.92           C  
ANISOU 1626  CG  PRO A 213     1051   1145   1194    130      6     51       C  
ATOM   1627  CD  PRO A 213      28.788  43.926  71.734  1.00  8.86           C  
ANISOU 1627  CD  PRO A 213     1043   1128   1194    121      1     40       C  
ATOM   1628  N   GLU A 214      32.102  43.931  73.423  1.00  8.58           N  
ANISOU 1628  N   GLU A 214     1015   1109   1137    122    -15     34       N  
ATOM   1629  CA  GLU A 214      33.419  43.564  73.928  1.00  8.94           C  
ANISOU 1629  CA  GLU A 214     1058   1161   1178    122    -22     35       C  
ATOM   1630  C   GLU A 214      34.514  44.538  73.502  1.00  9.03           C  
ANISOU 1630  C   GLU A 214     1074   1175   1183    114    -30     21       C  
ATOM   1631  O   GLU A 214      35.553  44.643  74.190  1.00  8.65           O  
ANISOU 1631  O   GLU A 214     1025   1135   1124    113    -37     20       O  
ATOM   1632  CB  GLU A 214      33.805  42.131  73.561  1.00  8.95           C  
ANISOU 1632  CB  GLU A 214     1049   1158   1195    122    -21     44       C  
ATOM   1633  CG  GLU A 214      33.912  41.816  72.085  1.00  9.32           C  
ANISOU 1633  CG  GLU A 214     1091   1194   1258    115    -21     38       C  
ATOM   1634  CD  GLU A 214      32.599  41.397  71.406  1.00  9.31           C  
ANISOU 1634  CD  GLU A 214     1088   1182   1268    113    -14     41       C  
ATOM   1635  OE1 GLU A 214      32.721  40.896  70.239  1.00  9.90           O  
ANISOU 1635  OE1 GLU A 214     1157   1247   1356    107    -14     37       O  
ATOM   1636  OE2 GLU A 214      31.488  41.591  71.994  1.00  9.65           O  
ANISOU 1636  OE2 GLU A 214     1133   1228   1307    117     -9     47       O  
ATOM   1637  N   ILE A 215      34.324  45.277  72.380  1.00  9.02           N  
ANISOU 1637  N   ILE A 215     1076   1165   1187    106    -31     11       N  
ATOM   1638  CA  ILE A 215      35.296  46.314  72.019  1.00  9.34           C  
ANISOU 1638  CA  ILE A 215     1122   1207   1221     98    -38     -2       C  
ATOM   1639  C   ILE A 215      35.530  47.306  73.142  1.00  9.40           C  
ANISOU 1639  C   ILE A 215     1140   1222   1209     99    -42     -7       C  
ATOM   1640  O   ILE A 215      36.638  47.826  73.312  1.00  9.97           O  
ANISOU 1640  O   ILE A 215     1214   1301   1275     91    -50    -14       O  
ATOM   1641  CB  ILE A 215      34.832  47.071  70.747  1.00 10.20           C  
ANISOU 1641  CB  ILE A 215     1235   1305   1336     92    -36    -11       C  
ATOM   1642  CG1 ILE A 215      34.844  46.086  69.590  1.00 11.15           C  
ANISOU 1642  CG1 ILE A 215     1345   1419   1473     89    -35     -8       C  
ATOM   1643  CG2 ILE A 215      35.672  48.350  70.507  1.00 10.68           C  
ANISOU 1643  CG2 ILE A 215     1304   1366   1389     82    -43    -23       C  
ATOM   1644  CD1 ILE A 215      36.210  45.573  69.255  1.00 12.46           C  
ANISOU 1644  CD1 ILE A 215     1503   1588   1643     84    -40    -10       C  
ATOM   1645  N   MET A 216      34.482  47.589  73.906  1.00  9.04           N  
ANISOU 1645  N   MET A 216     1102   1178   1156    107    -35     -4       N  
ATOM   1646  CA  MET A 216      34.541  48.601  74.974  1.00  9.26           C  
ANISOU 1646  CA  MET A 216     1142   1212   1165    108    -37    -11       C  
ATOM   1647  C   MET A 216      35.022  48.014  76.304  1.00  9.25           C  
ANISOU 1647  C   MET A 216     1138   1225   1152    114    -40     -3       C  
ATOM   1648  O   MET A 216      35.267  48.742  77.251  1.00  9.53           O  
ANISOU 1648  O   MET A 216     1184   1268   1170    114    -43     -9       O  
ATOM   1649  CB  MET A 216      33.189  49.304  75.117  1.00  9.86           C  
ANISOU 1649  CB  MET A 216     1228   1282   1237    116    -28    -12       C  
ATOM   1650  CG  MET A 216      32.912  50.333  73.995  1.00  9.97           C  
ANISOU 1650  CG  MET A 216     1249   1283   1257    110    -27    -22       C  
ATOM   1651  SD  MET A 216      32.442  49.589  72.429  1.00  9.72           S  
ANISOU 1651  SD  MET A 216     1205   1243   1247    107    -25    -17       S  
ATOM   1652  CE  MET A 216      30.802  49.123  72.762  1.00 10.41           C  
ANISOU 1652  CE  MET A 216     1288   1330   1337    120    -14     -5       C  
ATOM   1653  N   LEU A 217      35.112  46.693  76.380  1.00  9.49           N  
ANISOU 1653  N   LEU A 217     1156   1258   1192    118    -39     10       N  
ATOM   1654  CA  LEU A 217      35.372  45.934  77.610  1.00  9.67           C  
ANISOU 1654  CA  LEU A 217     1175   1294   1205    126    -40     22       C  
ATOM   1655  C   LEU A 217      36.702  45.284  77.630  1.00  9.58           C  
ANISOU 1655  C   LEU A 217     1154   1291   1196    122    -49     26       C  
ATOM   1656  O   LEU A 217      37.430  45.434  78.593  1.00 10.11           O  
ANISOU 1656  O   LEU A 217     1221   1371   1247    123    -56     26       O  
ATOM   1657  CB  LEU A 217      34.309  44.884  77.791  1.00  9.61           C  
ANISOU 1657  CB  LEU A 217     1162   1284   1207    135    -30     38       C  
ATOM   1658  CG  LEU A 217      32.896  45.486  77.989  1.00  9.79           C  
ANISOU 1658  CG  LEU A 217     1192   1302   1224    141    -20     37       C  
ATOM   1659  CD1 LEU A 217      31.856  44.377  77.868  1.00  9.48           C  
ANISOU 1659  CD1 LEU A 217     1144   1259   1199    147    -10     52       C  
ATOM   1660  CD2 LEU A 217      32.686  46.238  79.303  1.00 10.02           C  
ANISOU 1660  CD2 LEU A 217     1233   1344   1231    147    -18     34       C  
ATOM   1661  N   ASN A 218      37.033  44.538  76.572  1.00  9.29           N  
ANISOU 1661  N   ASN A 218     1107   1246   1178    120    -49     28       N  
ATOM   1662  CA  ASN A 218      38.221  43.663  76.640  1.00  9.25           C  
ANISOU 1662  CA  ASN A 218     1089   1247   1177    121    -55     36       C  
ATOM   1663  C   ASN A 218      38.782  43.143  75.299  1.00  9.21           C  
ANISOU 1663  C   ASN A 218     1076   1234   1191    116    -55     33       C  
ATOM   1664  O   ASN A 218      39.610  42.234  75.275  1.00  9.06           O  
ANISOU 1664  O   ASN A 218     1046   1218   1179    119    -58     41       O  
ATOM   1665  CB  ASN A 218      37.969  42.463  77.577  1.00  9.46           C  
ANISOU 1665  CB  ASN A 218     1111   1280   1204    132    -51     54       C  
ATOM   1666  CG  ASN A 218      36.974  41.496  77.004  1.00 10.84           C  
ANISOU 1666  CG  ASN A 218     1282   1441   1397    137    -40     63       C  
ATOM   1667  OD1 ASN A 218      36.415  41.735  75.940  1.00 11.24           O  
ANISOU 1667  OD1 ASN A 218     1333   1478   1458    131    -36     56       O  
ATOM   1668  ND2 ASN A 218      36.771  40.393  77.686  1.00 11.47           N  
ANISOU 1668  ND2 ASN A 218     1357   1522   1479    146    -36     80       N  
ATOM   1669  N   SER A 219      38.384  43.750  74.186  1.00  9.26           N  
ANISOU 1669  N   SER A 219     1085   1227   1204    108    -53     22       N  
ATOM   1670  CA  SER A 219      38.675  43.128  72.891  1.00  9.42           C  
ANISOU 1670  CA  SER A 219     1098   1239   1243    105    -51     21       C  
ATOM   1671  C   SER A 219      39.179  44.171  71.915  1.00  9.79           C  
ANISOU 1671  C   SER A 219     1147   1282   1289     93    -55      6       C  
ATOM   1672  O   SER A 219      38.616  45.222  71.779  1.00 10.03           O  
ANISOU 1672  O   SER A 219     1188   1309   1313     89    -54     -2       O  
ATOM   1673  CB  SER A 219      37.439  42.453  72.268  1.00  9.46           C  
ANISOU 1673  CB  SER A 219     1103   1229   1261    108    -41     25       C  
ATOM   1674  OG  SER A 219      37.757  41.891  70.986  1.00 10.02           O  
ANISOU 1674  OG  SER A 219     1168   1292   1348    104    -40     22       O  
ATOM   1675  N   LYS A 220      40.228  43.791  71.192  1.00 10.05           N  
ANISOU 1675  N   LYS A 220     1171   1317   1329     90    -58      4       N  
ATOM   1676  CA  LYS A 220      40.755  44.570  70.106  1.00 10.97           C  
ANISOU 1676  CA  LYS A 220     1288   1431   1449     79    -60     -8       C  
ATOM   1677  C   LYS A 220      39.993  44.316  68.792  1.00 10.61           C  
ANISOU 1677  C   LYS A 220     1244   1371   1416     77    -53    -11       C  
ATOM   1678  O   LYS A 220      40.379  44.928  67.755  1.00 11.59           O  
ANISOU 1678  O   LYS A 220     1369   1493   1542     68    -54    -20       O  
ATOM   1679  CB  LYS A 220      42.252  44.195  69.909  1.00 13.20           C  
ANISOU 1679  CB  LYS A 220     1558   1723   1733     77    -66     -7       C  
ATOM   1680  CG  LYS A 220      43.187  44.601  71.018  1.00 15.52           C  
ANISOU 1680  CG  LYS A 220     1850   2034   2014     75    -75     -6       C  
ATOM   1681  CD  LYS A 220      44.618  44.203  70.670  1.00 20.30           C  
ANISOU 1681  CD  LYS A 220     2439   2649   2623     73    -79     -4       C  
ATOM   1682  CE  LYS A 220      45.614  44.210  71.812  1.00 25.83           C  
ANISOU 1682  CE  LYS A 220     3132   3370   3312     75    -89      1       C  
ATOM   1683  NZ  LYS A 220      46.685  43.194  71.493  1.00 27.44           N  
ANISOU 1683  NZ  LYS A 220     3319   3582   3527     81    -89      9       N  
ATOM   1684  N   GLY A 221      39.052  43.373  68.741  1.00  9.89           N  
ANISOU 1684  N   GLY A 221     1152   1272   1334     84    -46     -4       N  
ATOM   1685  CA  GLY A 221      38.355  43.063  67.480  1.00  9.65           C  
ANISOU 1685  CA  GLY A 221     1122   1230   1316     82    -41     -7       C  
ATOM   1686  C   GLY A 221      39.167  42.236  66.534  1.00 10.02           C  
ANISOU 1686  C   GLY A 221     1160   1273   1374     81    -40     -9       C  
ATOM   1687  O   GLY A 221      39.089  42.472  65.309  1.00 11.78           O  
ANISOU 1687  O   GLY A 221     1383   1491   1601     74    -38    -17       O  
ATOM   1688  N   TYR A 222      39.883  41.253  67.061  1.00  9.75           N  
ANISOU 1688  N   TYR A 222     1118   1243   1344     88    -40     -1       N  
ATOM   1689  CA  TYR A 222      40.729  40.380  66.233  1.00  9.66           C  
ANISOU 1689  CA  TYR A 222     1098   1229   1344     90    -37     -2       C  
ATOM   1690  C   TYR A 222      40.131  38.989  66.034  1.00  9.57           C  
ANISOU 1690  C   TYR A 222     1085   1204   1346     97    -30      4       C  
ATOM   1691  O   TYR A 222      40.841  38.017  65.727  1.00  9.71           O  
ANISOU 1691  O   TYR A 222     1097   1220   1374    103    -27      6       O  
ATOM   1692  CB  TYR A 222      42.138  40.241  66.826  1.00 10.55           C  
ANISOU 1692  CB  TYR A 222     1202   1355   1453     94    -42      2       C  
ATOM   1693  CG  TYR A 222      42.975  41.497  66.897  1.00 10.76           C  
ANISOU 1693  CG  TYR A 222     1227   1394   1467     85    -50     -5       C  
ATOM   1694  CD1 TYR A 222      42.643  42.646  66.230  1.00 11.88           C  
ANISOU 1694  CD1 TYR A 222     1376   1533   1603     74    -51    -16       C  
ATOM   1695  CD2 TYR A 222      44.194  41.449  67.522  1.00 11.71           C  
ANISOU 1695  CD2 TYR A 222     1337   1528   1582     88    -56     -1       C  
ATOM   1696  CE1 TYR A 222      43.443  43.779  66.278  1.00 13.44           C  
ANISOU 1696  CE1 TYR A 222     1575   1741   1792     64    -57    -22       C  
ATOM   1697  CE2 TYR A 222      45.007  42.555  67.551  1.00 12.61           C  
ANISOU 1697  CE2 TYR A 222     1451   1655   1687     77    -63     -8       C  
ATOM   1698  CZ  TYR A 222      44.630  43.718  66.960  1.00 13.45           C  
ANISOU 1698  CZ  TYR A 222     1566   1757   1788     65    -64    -18       C  
ATOM   1699  OH  TYR A 222      45.502  44.815  67.011  1.00 16.57           O  
ANISOU 1699  OH  TYR A 222     1960   2162   2174     53    -71    -25       O  
ATOM   1700  N   THR A 223      38.790  38.834  66.185  1.00  9.22           N  
ANISOU 1700  N   THR A 223     1047   1152   1304     97    -27      7       N  
ATOM   1701  CA  THR A 223      38.163  37.536  65.905  1.00  9.62           C  
ANISOU 1701  CA  THR A 223     1098   1190   1370    100    -20     12       C  
ATOM   1702  C   THR A 223      36.931  37.745  65.032  1.00  9.02           C  
ANISOU 1702  C   THR A 223     1026   1104   1296     92    -17      6       C  
ATOM   1703  O   THR A 223      36.406  38.866  64.954  1.00  8.87           O  
ANISOU 1703  O   THR A 223     1011   1090   1268     86    -20      1       O  
ATOM   1704  CB  THR A 223      37.755  36.788  67.174  1.00 10.66           C  
ANISOU 1704  CB  THR A 223     1228   1320   1502    109    -17     27       C  
ATOM   1705  OG1 THR A 223      36.697  37.430  67.822  1.00 11.63           O  
ANISOU 1705  OG1 THR A 223     1356   1446   1617    107    -18     31       O  
ATOM   1706  CG2 THR A 223      38.929  36.699  68.120  1.00 11.29           C  
ANISOU 1706  CG2 THR A 223     1303   1412   1576    117    -21     35       C  
ATOM   1707  N   LYS A 224      36.491  36.682  64.382  1.00  8.79           N  
ANISOU 1707  N   LYS A 224      997   1063   1281     91    -12      5       N  
ATOM   1708  CA  LYS A 224      35.439  36.771  63.400  1.00  8.47           C  
ANISOU 1708  CA  LYS A 224      960   1015   1244     82    -11     -2       C  
ATOM   1709  C   LYS A 224      34.094  37.250  63.962  1.00  8.18           C  
ANISOU 1709  C   LYS A 224      925    981   1203     80    -11      4       C  
ATOM   1710  O   LYS A 224      33.290  37.892  63.253  1.00  8.15           O  
ANISOU 1710  O   LYS A 224      924    978   1197     72    -12     -2       O  
ATOM   1711  CB  LYS A 224      35.317  35.458  62.657  1.00  8.66           C  
ANISOU 1711  CB  LYS A 224      983   1024   1282     80     -5     -5       C  
ATOM   1712  CG  LYS A 224      36.522  35.193  61.750  1.00  9.00           C  
ANISOU 1712  CG  LYS A 224     1025   1066   1329     82     -5    -14       C  
ATOM   1713  CD  LYS A 224      36.579  33.792  61.183  1.00  9.41           C  
ANISOU 1713  CD  LYS A 224     1077   1102   1395     83      2    -17       C  
ATOM   1714  CE  LYS A 224      37.847  33.640  60.381  1.00  9.37           C  
ANISOU 1714  CE  LYS A 224     1071   1098   1391     87      4    -26       C  
ATOM   1715  NZ  LYS A 224      37.988  32.272  59.840  1.00  9.37           N  
ANISOU 1715  NZ  LYS A 224     1073   1081   1405     90     11    -30       N  
ATOM   1716  N   SER A 225      33.895  37.022  65.246  1.00  8.34           N  
ANISOU 1716  N   SER A 225      945   1004   1221     87     -9     16       N  
ATOM   1717  CA  SER A 225      32.708  37.500  65.917  1.00  8.31           C  
ANISOU 1717  CA  SER A 225      942   1004   1212     87     -8     23       C  
ATOM   1718  C   SER A 225      32.483  39.009  65.806  1.00  8.11           C  
ANISOU 1718  C   SER A 225      920    987   1172     84    -12     16       C  
ATOM   1719  O   SER A 225      31.343  39.461  65.961  1.00  8.43           O  
ANISOU 1719  O   SER A 225      963   1031   1211     83    -10     19       O  
ATOM   1720  CB  SER A 225      32.773  37.062  67.393  1.00  8.73           C  
ANISOU 1720  CB  SER A 225      994   1061   1262     96     -6     38       C  
ATOM   1721  OG  SER A 225      33.900  37.642  68.027  1.00 10.49           O  
ANISOU 1721  OG  SER A 225     1218   1294   1474    101    -10     37       O  
ATOM   1722  N   ILE A 226      33.550  39.789  65.601  1.00  8.09           N  
ANISOU 1722  N   ILE A 226      920    990   1162     84    -17      8       N  
ATOM   1723  CA  ILE A 226      33.423  41.220  65.493  1.00  8.92           C  
ANISOU 1723  CA  ILE A 226     1030   1102   1256     81    -20      2       C  
ATOM   1724  C   ILE A 226      32.559  41.604  64.295  1.00  8.30           C  
ANISOU 1724  C   ILE A 226      954   1020   1181     74    -20     -5       C  
ATOM   1725  O   ILE A 226      31.736  42.532  64.377  1.00  8.22           O  
ANISOU 1725  O   ILE A 226      947   1012   1164     74    -20     -5       O  
ATOM   1726  CB  ILE A 226      34.815  41.920  65.414  1.00  9.87           C  
ANISOU 1726  CB  ILE A 226     1153   1229   1369     79    -25     -6       C  
ATOM   1727  CG1 ILE A 226      34.687  43.372  65.748  1.00 12.25           C  
ANISOU 1727  CG1 ILE A 226     1461   1535   1657     77    -28    -10       C  
ATOM   1728  CG2 ILE A 226      35.524  41.760  64.083  1.00 10.64           C  
ANISOU 1728  CG2 ILE A 226     1248   1323   1473     73    -26    -15       C  
ATOM   1729  CD1 ILE A 226      34.334  43.580  67.164  1.00 13.81           C  
ANISOU 1729  CD1 ILE A 226     1662   1739   1846     85    -28     -2       C  
ATOM   1730  N   ASP A 227      32.717  40.883  63.189  1.00  7.79           N  
ANISOU 1730  N   ASP A 227      886    948   1125     68    -19    -10       N  
ATOM   1731  CA  ASP A 227      31.984  41.204  61.998  1.00  7.50           C  
ANISOU 1731  CA  ASP A 227      850    910   1091     61    -20    -16       C  
ATOM   1732  C   ASP A 227      30.543  40.713  62.079  1.00  7.46           C  
ANISOU 1732  C   ASP A 227      841    901   1091     60    -17     -9       C  
ATOM   1733  O   ASP A 227      29.616  41.353  61.559  1.00  7.63           O  
ANISOU 1733  O   ASP A 227      863    926   1109     58    -18    -10       O  
ATOM   1734  CB  ASP A 227      32.667  40.549  60.791  1.00  7.39           C  
ANISOU 1734  CB  ASP A 227      834    891   1083     56    -20    -25       C  
ATOM   1735  CG  ASP A 227      33.946  41.268  60.342  1.00  7.51           C  
ANISOU 1735  CG  ASP A 227      851    910   1091     54    -23    -33       C  
ATOM   1736  OD1 ASP A 227      34.061  42.494  60.514  1.00  7.09           O  
ANISOU 1736  OD1 ASP A 227      802    863   1028     53    -26    -34       O  
ATOM   1737  OD2 ASP A 227      34.772  40.565  59.691  1.00  8.26           O  
ANISOU 1737  OD2 ASP A 227      943   1002   1192     53    -21    -38       O  
ATOM   1738  N   ILE A 228      30.330  39.581  62.720  1.00  7.96           N  
ANISOU 1738  N   ILE A 228      901    960   1163     63    -13     -2       N  
ATOM   1739  CA  ILE A 228      28.978  39.094  62.903  1.00  8.54           C  
ANISOU 1739  CA  ILE A 228      970   1032   1242     61    -10      6       C  
ATOM   1740  C   ILE A 228      28.114  40.062  63.708  1.00  8.18           C  
ANISOU 1740  C   ILE A 228      926    996   1188     67     -9     13       C  
ATOM   1741  O   ILE A 228      26.951  40.352  63.346  1.00  7.89           O  
ANISOU 1741  O   ILE A 228      886    962   1152     64     -9     15       O  
ATOM   1742  CB  ILE A 228      28.977  37.684  63.502  1.00  9.14           C  
ANISOU 1742  CB  ILE A 228     1043   1100   1329     62     -6     15       C  
ATOM   1743  CG1 ILE A 228      29.681  36.700  62.547  1.00 10.10           C  
ANISOU 1743  CG1 ILE A 228     1165   1211   1461     57     -6      6       C  
ATOM   1744  CG2 ILE A 228      27.557  37.199  63.794  1.00  9.35           C  
ANISOU 1744  CG2 ILE A 228     1064   1125   1362     59     -2     24       C  
ATOM   1745  CD1 ILE A 228      28.918  36.360  61.291  1.00 11.46           C  
ANISOU 1745  CD1 ILE A 228     1336   1378   1640     45     -7     -2       C  
ATOM   1746  N   TRP A 229      28.687  40.655  64.741  1.00  8.09           N  
ANISOU 1746  N   TRP A 229      918    989   1167     75     -9     16       N  
ATOM   1747  CA  TRP A 229      27.977  41.688  65.488  1.00  7.59           C  
ANISOU 1747  CA  TRP A 229      858    934   1093     81     -7     20       C  
ATOM   1748  C   TRP A 229      27.518  42.828  64.552  1.00  7.75           C  
ANISOU 1748  C   TRP A 229      881    957   1109     79    -10     13       C  
ATOM   1749  O   TRP A 229      26.365  43.236  64.582  1.00  7.80           O  
ANISOU 1749  O   TRP A 229      885    966   1113     81     -7     18       O  
ATOM   1750  CB  TRP A 229      28.854  42.275  66.606  1.00  7.81           C  
ANISOU 1750  CB  TRP A 229      892    966   1109     89     -8     21       C  
ATOM   1751  CG  TRP A 229      28.124  43.343  67.354  1.00  7.34           C  
ANISOU 1751  CG  TRP A 229      837    914   1038     96     -5     24       C  
ATOM   1752  CD1 TRP A 229      28.087  44.703  67.048  1.00  7.59           C  
ANISOU 1752  CD1 TRP A 229      876    947   1060     97     -7     16       C  
ATOM   1753  CD2 TRP A 229      27.248  43.195  68.474  1.00  7.65           C  
ANISOU 1753  CD2 TRP A 229      874    958   1073    104      1     35       C  
ATOM   1754  NE1 TRP A 229      27.267  45.349  67.872  1.00  7.51           N  
ANISOU 1754  NE1 TRP A 229      869    941   1042    105     -3     21       N  
ATOM   1755  CE2 TRP A 229      26.726  44.471  68.755  1.00  7.60           C  
ANISOU 1755  CE2 TRP A 229      875    957   1057    110      3     32       C  
ATOM   1756  CE3 TRP A 229      26.820  42.101  69.257  1.00  7.89           C  
ANISOU 1756  CE3 TRP A 229      899    990   1110    106      6     47       C  
ATOM   1757  CZ2 TRP A 229      25.802  44.702  69.763  1.00  7.95           C  
ANISOU 1757  CZ2 TRP A 229      920   1008   1095    119     10     40       C  
ATOM   1758  CZ3 TRP A 229      25.908  42.355  70.292  1.00  8.29           C  
ANISOU 1758  CZ3 TRP A 229      949   1048   1153    115     13     57       C  
ATOM   1759  CH2 TRP A 229      25.423  43.657  70.528  1.00  8.42           C  
ANISOU 1759  CH2 TRP A 229      972   1070   1158    122     15     53       C  
ATOM   1760  N   SER A 230      28.453  43.316  63.735  1.00  7.37           N  
ANISOU 1760  N   SER A 230      837    906   1057     74    -15      3       N  
ATOM   1761  CA  SER A 230      28.113  44.425  62.848  1.00  7.23           C  
ANISOU 1761  CA  SER A 230      823    890   1035     72    -17     -3       C  
ATOM   1762  C   SER A 230      27.016  44.031  61.870  1.00  7.15           C  
ANISOU 1762  C   SER A 230      806    880   1032     67    -17     -1       C  
ATOM   1763  O   SER A 230      26.135  44.781  61.564  1.00  7.09           O  
ANISOU 1763  O   SER A 230      798    876   1021     69    -17      1       O  
ATOM   1764  CB  SER A 230      29.338  44.882  62.048  1.00  7.64           C  
ANISOU 1764  CB  SER A 230      880    940   1084     66    -22    -13       C  
ATOM   1765  OG  SER A 230      30.401  45.278  62.931  1.00  8.82           O  
ANISOU 1765  OG  SER A 230     1034   1090   1226     69    -23    -15       O  
ATOM   1766  N   VAL A 231      27.056  42.824  61.371  1.00  6.75           N  
ANISOU 1766  N   VAL A 231      749    825    991     60    -18     -2       N  
ATOM   1767  CA  VAL A 231      25.979  42.325  60.508  1.00  7.45           C  
ANISOU 1767  CA  VAL A 231      831    914   1087     53    -19     -1       C  
ATOM   1768  C   VAL A 231      24.661  42.342  61.222  1.00  7.48           C  
ANISOU 1768  C   VAL A 231      827    922   1091     57    -15     10       C  
ATOM   1769  O   VAL A 231      23.643  42.716  60.641  1.00  7.74           O  
ANISOU 1769  O   VAL A 231      855    961   1123     55    -16     12       O  
ATOM   1770  CB  VAL A 231      26.267  40.945  59.891  1.00  7.83           C  
ANISOU 1770  CB  VAL A 231      875    954   1145     43    -19     -6       C  
ATOM   1771  CG1 VAL A 231      25.061  40.476  59.052  1.00  8.04           C  
ANISOU 1771  CG1 VAL A 231      894    982   1177     34    -21     -5       C  
ATOM   1772  CG2 VAL A 231      27.505  41.031  59.015  1.00  8.33           C  
ANISOU 1772  CG2 VAL A 231      944   1015   1207     40    -22    -18       C  
ATOM   1773  N   GLY A 232      24.641  41.875  62.447  1.00  7.58           N  
ANISOU 1773  N   GLY A 232      839    935   1105     63    -10     18       N  
ATOM   1774  CA  GLY A 232      23.404  41.934  63.253  1.00  7.61           C  
ANISOU 1774  CA  GLY A 232      837    945   1109     68     -5     30       C  
ATOM   1775  C   GLY A 232      22.875  43.342  63.396  1.00  7.72           C  
ANISOU 1775  C   GLY A 232      854    967   1113     78     -4     31       C  
ATOM   1776  O   GLY A 232      21.690  43.617  63.204  1.00  7.85           O  
ANISOU 1776  O   GLY A 232      863    990   1130     79     -2     37       O  
ATOM   1777  N   CYS A 233      23.784  44.294  63.604  1.00  7.24           N  
ANISOU 1777  N   CYS A 233      804    905   1042     83     -5     25       N  
ATOM   1778  CA  CYS A 233      23.391  45.727  63.633  1.00  7.87           C  
ANISOU 1778  CA  CYS A 233      890    989   1112     92     -5     24       C  
ATOM   1779  C   CYS A 233      22.776  46.185  62.302  1.00  7.69           C  
ANISOU 1779  C   CYS A 233      864    968   1091     88     -9     22       C  
ATOM   1780  O   CYS A 233      21.790  46.954  62.261  1.00  8.04           O  
ANISOU 1780  O   CYS A 233      905   1018   1131     95     -7     27       O  
ATOM   1781  CB  CYS A 233      24.560  46.641  63.941  1.00  8.05           C  
ANISOU 1781  CB  CYS A 233      927   1008   1125     95     -6     16       C  
ATOM   1782  SG  CYS A 233      25.203  46.426  65.628  1.00  9.33           S  
ANISOU 1782  SG  CYS A 233     1094   1170   1281    102     -2     19       S  
ATOM   1783  N   ILE A 234      23.349  45.704  61.191  1.00  7.81           N  
ANISOU 1783  N   ILE A 234      878    979   1110     76    -15     14       N  
ATOM   1784  CA  ILE A 234      22.844  46.027  59.858  1.00  7.78           C  
ANISOU 1784  CA  ILE A 234      871    979   1107     71    -19     12       C  
ATOM   1785  C   ILE A 234      21.476  45.409  59.642  1.00  7.45           C  
ANISOU 1785  C   ILE A 234      814    944   1071     68    -19     20       C  
ATOM   1786  O   ILE A 234      20.593  46.053  59.054  1.00  8.81           O  
ANISOU 1786  O   ILE A 234      982   1124   1241     71    -21     24       O  
ATOM   1787  CB  ILE A 234      23.823  45.610  58.778  1.00  8.10           C  
ANISOU 1787  CB  ILE A 234      914   1014   1149     60    -25      2       C  
ATOM   1788  CG1 ILE A 234      25.108  46.476  58.889  1.00  7.93           C  
ANISOU 1788  CG1 ILE A 234      905    988   1120     62    -25     -6       C  
ATOM   1789  CG2 ILE A 234      23.246  45.789  57.379  1.00  8.09           C  
ANISOU 1789  CG2 ILE A 234      908   1018   1147     53    -30      0       C  
ATOM   1790  CD1 ILE A 234      26.343  45.862  58.282  1.00  8.70           C  
ANISOU 1790  CD1 ILE A 234     1005   1081   1221     53    -28    -15       C  
ATOM   1791  N   LEU A 235      21.294  44.155  60.041  1.00  7.51           N  
ANISOU 1791  N   LEU A 235      815    950   1089     62    -17     23       N  
ATOM   1792  CA  LEU A 235      19.978  43.561  59.934  1.00  7.92           C  
ANISOU 1792  CA  LEU A 235      853   1010   1148     58    -17     32       C  
ATOM   1793  C   LEU A 235      18.928  44.346  60.690  1.00  8.32           C  
ANISOU 1793  C   LEU A 235      898   1069   1193     71    -11     44       C  
ATOM   1794  O   LEU A 235      17.841  44.652  60.156  1.00  8.35           O  
ANISOU 1794  O   LEU A 235      892   1083   1197     71    -13     49       O  
ATOM   1795  CB  LEU A 235      20.060  42.116  60.427  1.00  8.04           C  
ANISOU 1795  CB  LEU A 235      864   1019   1173     50    -14     34       C  
ATOM   1796  CG  LEU A 235      18.704  41.379  60.502  1.00  8.55           C  
ANISOU 1796  CG  LEU A 235      913   1090   1246     43    -13     44       C  
ATOM   1797  CD1 LEU A 235      18.018  41.351  59.120  1.00  9.09           C  
ANISOU 1797  CD1 LEU A 235      973   1164   1316     32    -21     41       C  
ATOM   1798  CD2 LEU A 235      18.949  39.936  61.005  1.00  9.55           C  
ANISOU 1798  CD2 LEU A 235     1037   1206   1384     35     -9     46       C  
ATOM   1799  N   ALA A 236      19.217  44.712  61.926  1.00  8.35           N  
ANISOU 1799  N   ALA A 236      909   1072   1193     82     -4     47       N  
ATOM   1800  CA  ALA A 236      18.282  45.506  62.736  1.00  9.01           C  
ANISOU 1800  CA  ALA A 236      989   1164   1270     97      3     57       C  
ATOM   1801  C   ALA A 236      17.911  46.802  62.028  1.00  9.12           C  
ANISOU 1801  C   ALA A 236     1006   1182   1277    105      0     56       C  
ATOM   1802  O   ALA A 236      16.773  47.241  61.997  1.00  9.01           O  
ANISOU 1802  O   ALA A 236      983   1178   1263    112      3     65       O  
ATOM   1803  CB  ALA A 236      18.884  45.787  64.127  1.00  9.32           C  
ANISOU 1803  CB  ALA A 236     1039   1199   1302    107     10     58       C  
ATOM   1804  N   GLU A 237      18.907  47.433  61.466  1.00  8.98           N  
ANISOU 1804  N   GLU A 237     1001   1157   1255    103     -4     46       N  
ATOM   1805  CA  GLU A 237      18.725  48.675  60.772  1.00  9.55           C  
ANISOU 1805  CA  GLU A 237     1079   1230   1321    110     -7     45       C  
ATOM   1806  C   GLU A 237      17.885  48.486  59.502  1.00  9.38           C  
ANISOU 1806  C   GLU A 237     1044   1217   1302    103    -13     48       C  
ATOM   1807  O   GLU A 237      17.065  49.370  59.146  1.00  9.52           O  
ANISOU 1807  O   GLU A 237     1058   1241   1316    113    -13     55       O  
ATOM   1808  CB  GLU A 237      20.087  49.293  60.487  1.00  9.94           C  
ANISOU 1808  CB  GLU A 237     1144   1268   1363    107    -10     33       C  
ATOM   1809  CG  GLU A 237      20.076  50.695  59.987  1.00 10.56           C  
ANISOU 1809  CG  GLU A 237     1233   1345   1435    116    -11     32       C  
ATOM   1810  CD  GLU A 237      21.364  51.466  60.247  1.00 10.39           C  
ANISOU 1810  CD  GLU A 237     1229   1312   1407    116    -11     23       C  
ATOM   1811  OE1 GLU A 237      22.311  51.022  60.945  1.00 10.20           O  
ANISOU 1811  OE1 GLU A 237     1210   1283   1382    111    -10     17       O  
ATOM   1812  OE2 GLU A 237      21.446  52.591  59.723  1.00 12.51           O  
ANISOU 1812  OE2 GLU A 237     1507   1576   1670    120    -11     22       O  
ATOM   1813  N   MET A 238      18.018  47.362  58.803  1.00  8.92           N  
ANISOU 1813  N   MET A 238      979   1160   1252     87    -19     44       N  
ATOM   1814  CA  MET A 238      17.171  47.062  57.633  1.00  9.86           C  
ANISOU 1814  CA  MET A 238     1085   1288   1373     78    -26     47       C  
ATOM   1815  C   MET A 238      15.721  46.822  58.057  1.00 10.51           C  
ANISOU 1815  C   MET A 238     1150   1384   1460     83    -23     60       C  
ATOM   1816  O   MET A 238      14.808  47.169  57.306  1.00 11.53           O  
ANISOU 1816  O   MET A 238     1267   1524   1588     83    -27     66       O  
ATOM   1817  CB  MET A 238      17.671  45.837  56.867  1.00  9.31           C  
ANISOU 1817  CB  MET A 238     1013   1215   1310     60    -33     38       C  
ATOM   1818  CG  MET A 238      18.959  46.064  56.081  1.00  9.32           C  
ANISOU 1818  CG  MET A 238     1027   1207   1306     54    -37     25       C  
ATOM   1819  SD  MET A 238      19.318  44.864  54.819  1.00  9.89           S  
ANISOU 1819  SD  MET A 238     1097   1278   1383     34    -45     13       S  
ATOM   1820  CE  MET A 238      19.848  43.501  55.794  1.00  9.99           C  
ANISOU 1820  CE  MET A 238     1110   1280   1407     29    -39     11       C  
ATOM   1821  N   LEU A 239      15.532  46.277  59.257  1.00 10.07           N  
ANISOU 1821  N   LEU A 239     1091   1327   1409     86    -15     66       N  
ATOM   1822  CA  LEU A 239      14.182  45.972  59.776  1.00 11.29           C  
ANISOU 1822  CA  LEU A 239     1227   1494   1568     89    -10     79       C  
ATOM   1823  C   LEU A 239      13.466  47.256  60.126  1.00 12.00           C  
ANISOU 1823  C   LEU A 239     1316   1592   1650    109     -5     88       C  
ATOM   1824  O   LEU A 239      12.247  47.335  59.932  1.00 14.00           O  
ANISOU 1824  O   LEU A 239     1553   1861   1906    113     -4     99       O  
ATOM   1825  CB  LEU A 239      14.249  45.054  60.959  1.00 11.54           C  
ANISOU 1825  CB  LEU A 239     1257   1522   1605     87     -3     84       C  
ATOM   1826  CG  LEU A 239      14.731  43.622  60.662  1.00 12.32           C  
ANISOU 1826  CG  LEU A 239     1354   1612   1714     67     -7     77       C  
ATOM   1827  CD1 LEU A 239      15.009  42.943  61.979  1.00 14.97           C  
ANISOU 1827  CD1 LEU A 239     1693   1943   2054     70      2     82       C  
ATOM   1828  CD2 LEU A 239      13.851  42.769  59.801  1.00 13.52           C  
ANISOU 1828  CD2 LEU A 239     1490   1772   1874     51    -14     80       C  
ATOM   1829  N   SER A 240      14.173  48.244  60.649  1.00 12.20           N  
ANISOU 1829  N   SER A 240     1359   1609   1668    123      0     84       N  
ATOM   1830  CA  SER A 240      13.511  49.427  61.260  1.00 12.22           C  
ANISOU 1830  CA  SER A 240     1364   1617   1664    145      9     92       C  
ATOM   1831  C   SER A 240      13.841  50.763  60.634  1.00 11.24           C  
ANISOU 1831  C   SER A 240     1252   1486   1531    155      6     88       C  
ATOM   1832  O   SER A 240      13.290  51.780  61.041  1.00 11.86           O  
ANISOU 1832  O   SER A 240     1334   1568   1606    173     13     94       O  
ATOM   1833  CB  SER A 240      13.931  49.505  62.732  1.00 13.69           C  
ANISOU 1833  CB  SER A 240     1560   1796   1846    154     19     91       C  
ATOM   1834  OG  SER A 240      15.338  49.732  62.805  1.00 16.77           O  
ANISOU 1834  OG  SER A 240     1970   2171   2231    150     16     78       O  
ATOM   1835  N   ASN A 241      14.771  50.793  59.678  1.00 10.65           N  
ANISOU 1835  N   ASN A 241     1188   1404   1456    143     -3     78       N  
ATOM   1836  CA  ASN A 241      15.266  52.018  59.075  1.00 11.43           C  
ANISOU 1836  CA  ASN A 241     1301   1495   1548    150     -5     73       C  
ATOM   1837  C   ASN A 241      15.887  53.002  60.074  1.00 12.42           C  
ANISOU 1837  C   ASN A 241     1446   1608   1666    164      4     69       C  
ATOM   1838  O   ASN A 241      15.865  54.188  59.844  1.00 14.64           O  
ANISOU 1838  O   ASN A 241     1737   1883   1941    175      5     70       O  
ATOM   1839  CB  ASN A 241      14.167  52.715  58.283  1.00 11.68           C  
ANISOU 1839  CB  ASN A 241     1322   1538   1578    160     -7     84       C  
ATOM   1840  CG  ASN A 241      13.762  51.942  57.045  1.00 11.35           C  
ANISOU 1840  CG  ASN A 241     1264   1508   1540    144    -18     86       C  
ATOM   1841  OD1 ASN A 241      12.923  51.063  57.114  1.00 12.55           O  
ANISOU 1841  OD1 ASN A 241     1398   1672   1698    138    -19     92       O  
ATOM   1842  ND2 ASN A 241      14.329  52.268  55.933  1.00 10.98           N  
ANISOU 1842  ND2 ASN A 241     1224   1458   1489    137    -26     80       N  
ATOM   1843  N   ARG A 242      16.458  52.512  61.158  1.00 12.39           N  
ANISOU 1843  N   ARG A 242     1447   1598   1661    162      8     64       N  
ATOM   1844  CA  ARG A 242      17.253  53.346  62.041  1.00 13.03           C  
ANISOU 1844  CA  ARG A 242     1548   1668   1735    170     14     57       C  
ATOM   1845  C   ARG A 242      18.310  52.503  62.710  1.00 12.23           C  
ANISOU 1845  C   ARG A 242     1452   1561   1634    159     13     48       C  
ATOM   1846  O   ARG A 242      18.152  51.316  62.863  1.00 11.20           O  
ANISOU 1846  O   ARG A 242     1309   1436   1510    150     12     51       O  
ATOM   1847  CB  ARG A 242      16.397  54.020  63.115  1.00 17.09           C  
ANISOU 1847  CB  ARG A 242     2064   2185   2244    191     25     64       C  
ATOM   1848  CG  ARG A 242      15.682  53.018  64.000  1.00 20.74           C  
ANISOU 1848  CG  ARG A 242     2510   2658   2710    192     31     72       C  
ATOM   1849  CD  ARG A 242      14.831  53.667  65.107  1.00 28.34           C  
ANISOU 1849  CD  ARG A 242     3474   3625   3667    213     44     79       C  
ATOM   1850  NE  ARG A 242      15.560  53.688  66.387  1.00 39.51           N  
ANISOU 1850  NE  ARG A 242     4903   5034   5074    216     50     71       N  
ATOM   1851  CZ  ARG A 242      15.015  53.483  67.596  1.00 47.92           C  
ANISOU 1851  CZ  ARG A 242     5966   6107   6135    227     61     77       C  
ATOM   1852  NH1 ARG A 242      15.785  53.534  68.679  1.00 54.43           N  
ANISOU 1852  NH1 ARG A 242     6805   6926   6951    228     65     70       N  
ATOM   1853  NH2 ARG A 242      13.715  53.213  67.741  1.00 50.79           N  
ANISOU 1853  NH2 ARG A 242     6311   6485   6503    235     68     91       N  
ATOM   1854  N   PRO A 243      19.444  53.090  63.024  1.00 10.54           N  
ANISOU 1854  N   PRO A 243     1256   1336   1414    158     12     38       N  
ATOM   1855  CA  PRO A 243      20.464  52.298  63.720  1.00 10.55           C  
ANISOU 1855  CA  PRO A 243     1261   1334   1415    149     11     31       C  
ATOM   1856  C   PRO A 243      19.978  51.805  65.056  1.00 10.20           C  
ANISOU 1856  C   PRO A 243     1212   1295   1369    157     19     37       C  
ATOM   1857  O   PRO A 243      19.294  52.535  65.769  1.00 10.58           O  
ANISOU 1857  O   PRO A 243     1264   1345   1411    172     27     41       O  
ATOM   1858  CB  PRO A 243      21.628  53.260  63.922  1.00 11.77           C  
ANISOU 1858  CB  PRO A 243     1435   1476   1562    148      9     20       C  
ATOM   1859  CG  PRO A 243      21.106  54.627  63.627  1.00 13.21           C  
ANISOU 1859  CG  PRO A 243     1627   1655   1740    160     12     22       C  
ATOM   1860  CD  PRO A 243      19.856  54.488  62.790  1.00 12.11           C  
ANISOU 1860  CD  PRO A 243     1471   1523   1606    165     12     33       C  
ATOM   1861  N   ILE A 244      20.301  50.552  65.385  1.00  9.48           N  
ANISOU 1861  N   ILE A 244     1112   1206   1283    147     17     39       N  
ATOM   1862  CA  ILE A 244      19.819  49.963  66.638  1.00  9.68           C  
ANISOU 1862  CA  ILE A 244     1133   1239   1308    154     25     46       C  
ATOM   1863  C   ILE A 244      20.493  50.583  67.892  1.00  9.49           C  
ANISOU 1863  C   ILE A 244     1124   1211   1271    162     29     41       C  
ATOM   1864  O   ILE A 244      19.847  50.726  68.952  1.00  9.68           O  
ANISOU 1864  O   ILE A 244     1148   1241   1288    174     38     47       O  
ATOM   1865  CB  ILE A 244      19.855  48.433  66.628  1.00 10.26           C  
ANISOU 1865  CB  ILE A 244     1192   1314   1390    142     23     51       C  
ATOM   1866  CG1 ILE A 244      19.352  47.918  67.948  1.00 11.00           C  
ANISOU 1866  CG1 ILE A 244     1282   1416   1482    149     32     61       C  
ATOM   1867  CG2 ILE A 244      21.234  47.927  66.286  1.00  9.77           C  
ANISOU 1867  CG2 ILE A 244     1137   1244   1331    130     15     42       C  
ATOM   1868  CD1 ILE A 244      19.142  46.451  67.957  1.00 11.55           C  
ANISOU 1868  CD1 ILE A 244     1338   1487   1563    139     31     69       C  
ATOM   1869  N   PHE A 245      21.792  50.860  67.788  1.00  9.20           N  
ANISOU 1869  N   PHE A 245     1100   1166   1230    155     23     30       N  
ATOM   1870  CA  PHE A 245      22.599  51.316  68.932  1.00  9.26           C  
ANISOU 1870  CA  PHE A 245     1122   1171   1226    159     25     23       C  
ATOM   1871  C   PHE A 245      23.375  52.618  68.555  1.00  9.41           C  
ANISOU 1871  C   PHE A 245     1158   1180   1238    158     20     11       C  
ATOM   1872  O   PHE A 245      24.589  52.590  68.288  1.00  9.21           O  
ANISOU 1872  O   PHE A 245     1138   1150   1212    146     13      2       O  
ATOM   1873  CB  PHE A 245      23.615  50.275  69.338  1.00  9.40           C  
ANISOU 1873  CB  PHE A 245     1137   1191   1245    149     20     22       C  
ATOM   1874  CG  PHE A 245      23.040  48.914  69.685  1.00  9.65           C  
ANISOU 1874  CG  PHE A 245     1154   1229   1285    148     23     34       C  
ATOM   1875  CD1 PHE A 245      22.104  48.747  70.694  1.00 10.62           C  
ANISOU 1875  CD1 PHE A 245     1272   1360   1403    159     33     44       C  
ATOM   1876  CD2 PHE A 245      23.444  47.778  68.963  1.00  9.38           C  
ANISOU 1876  CD2 PHE A 245     1109   1192   1262    136     18     35       C  
ATOM   1877  CE1 PHE A 245      21.629  47.455  70.966  1.00 10.40           C  
ANISOU 1877  CE1 PHE A 245     1231   1338   1384    156     36     56       C  
ATOM   1878  CE2 PHE A 245      22.925  46.515  69.218  1.00 10.54           C  
ANISOU 1878  CE2 PHE A 245     1244   1343   1418    133     21     46       C  
ATOM   1879  CZ  PHE A 245      22.058  46.369  70.235  1.00 10.59           C  
ANISOU 1879  CZ  PHE A 245     1246   1357   1420    143     30     56       C  
ATOM   1880  N   PRO A 246      22.669  53.757  68.466  1.00 10.49           N  
ANISOU 1880  N   PRO A 246     1302   1313   1370    169     26     10       N  
ATOM   1881  CA  PRO A 246      23.318  54.991  68.035  1.00 11.27           C  
ANISOU 1881  CA  PRO A 246     1417   1400   1464    167     22      0       C  
ATOM   1882  C   PRO A 246      24.025  55.741  69.193  1.00 11.57           C  
ANISOU 1882  C   PRO A 246     1475   1433   1489    170     24    -10       C  
ATOM   1883  O   PRO A 246      23.630  56.876  69.556  1.00 12.46           O  
ANISOU 1883  O   PRO A 246     1601   1539   1593    181     30    -14       O  
ATOM   1884  CB  PRO A 246      22.146  55.780  67.476  1.00 11.44           C  
ANISOU 1884  CB  PRO A 246     1439   1420   1488    180     28      6       C  
ATOM   1885  CG  PRO A 246      21.029  55.391  68.298  1.00 12.02           C  
ANISOU 1885  CG  PRO A 246     1503   1503   1560    193     37     16       C  
ATOM   1886  CD  PRO A 246      21.210  53.910  68.573  1.00 11.74           C  
ANISOU 1886  CD  PRO A 246     1453   1478   1530    183     35     21       C  
ATOM   1887  N   GLY A 247      25.090  55.180  69.752  1.00 11.20           N  
ANISOU 1887  N   GLY A 247     1429   1389   1438    160     19    -15       N  
ATOM   1888  CA  GLY A 247      25.793  55.847  70.873  1.00 12.94           C  
ANISOU 1888  CA  GLY A 247     1666   1607   1644    161     19    -25       C  
ATOM   1889  C   GLY A 247      26.311  57.207  70.441  1.00 14.30           C  
ANISOU 1889  C   GLY A 247     1857   1765   1813    158     16    -37       C  
ATOM   1890  O   GLY A 247      26.827  57.365  69.316  1.00 14.40           O  
ANISOU 1890  O   GLY A 247     1867   1771   1832    147     10    -39       O  
ATOM   1891  N   LYS A 248      26.256  58.166  71.364  1.00 15.48           N  
ANISOU 1891  N   LYS A 248     2024   1909   1950    165     21    -45       N  
ATOM   1892  CA  LYS A 248      26.668  59.553  71.126  1.00 18.09           C  
ANISOU 1892  CA  LYS A 248     2374   2223   2275    163     21    -56       C  
ATOM   1893  C   LYS A 248      28.105  59.807  71.499  1.00 18.05           C  
ANISOU 1893  C   LYS A 248     2380   2216   2263    146     11    -69       C  
ATOM   1894  O   LYS A 248      28.632  60.874  71.206  1.00 18.67           O  
ANISOU 1894  O   LYS A 248     2474   2280   2339    139      9    -78       O  
ATOM   1895  CB  LYS A 248      25.798  60.473  71.956  1.00 19.69           C  
ANISOU 1895  CB  LYS A 248     2592   2420   2468    181     32    -59       C  
ATOM   1896  CG  LYS A 248      24.326  60.439  71.627  1.00 23.00           C  
ANISOU 1896  CG  LYS A 248     3003   2843   2894    199     42    -47       C  
ATOM   1897  CD  LYS A 248      23.518  61.508  72.358  1.00 27.60           C  
ANISOU 1897  CD  LYS A 248     3602   3417   3466    219     54    -51       C  
ATOM   1898  CE  LYS A 248      22.073  61.429  71.852  1.00 31.68           C  
ANISOU 1898  CE  LYS A 248     4105   3939   3992    237     64    -36       C  
ATOM   1899  NZ  LYS A 248      21.127  62.431  72.401  1.00 36.16           N  
ANISOU 1899  NZ  LYS A 248     4686   4499   4552    259     77    -37       N  
ATOM   1900  N   HIS A 249      28.737  58.841  72.145  1.00 17.09           N  
ANISOU 1900  N   HIS A 249     2248   2107   2138    140      6    -68       N  
ATOM   1901  CA  HIS A 249      30.127  58.878  72.511  1.00 16.23           C  
ANISOU 1901  CA  HIS A 249     2143   2000   2022    124     -4    -78       C  
ATOM   1902  C   HIS A 249      30.510  57.480  72.912  1.00 15.52           C  
ANISOU 1902  C   HIS A 249     2036   1926   1933    121     -8    -70       C  
ATOM   1903  O   HIS A 249      29.668  56.569  72.942  1.00 15.38           O  
ANISOU 1903  O   HIS A 249     2005   1917   1922    131     -3    -58       O  
ATOM   1904  CB  HIS A 249      30.399  59.900  73.659  1.00 16.57           C  
ANISOU 1904  CB  HIS A 249     2209   2038   2048    125     -3    -91       C  
ATOM   1905  CG  HIS A 249      29.553  59.714  74.885  1.00 16.98           C  
ANISOU 1905  CG  HIS A 249     2264   2099   2089    141      6    -89       C  
ATOM   1906  ND1 HIS A 249      29.850  58.804  75.878  1.00 19.36           N  
ANISOU 1906  ND1 HIS A 249     2558   2417   2382    142      3    -86       N  
ATOM   1907  CD2 HIS A 249      28.471  60.397  75.314  1.00 18.66           C  
ANISOU 1907  CD2 HIS A 249     2489   2305   2295    159     18    -90       C  
ATOM   1908  CE1 HIS A 249      28.982  58.940  76.867  1.00 19.52           C  
ANISOU 1908  CE1 HIS A 249     2585   2442   2391    158     13    -85       C  
ATOM   1909  NE2 HIS A 249      28.111  59.868  76.529  1.00 19.47           N  
ANISOU 1909  NE2 HIS A 249     2590   2422   2387    169     22    -87       N  
ATOM   1910  N   TYR A 250      31.780  57.282  73.164  1.00 15.95           N  
ANISOU 1910  N   TYR A 250     2089   1986   1984    107    -18    -76       N  
ATOM   1911  CA  TYR A 250      32.383  55.958  73.312  1.00 13.89           C  
ANISOU 1911  CA  TYR A 250     1811   1739   1728    102    -24    -68       C  
ATOM   1912  C   TYR A 250      31.672  55.040  74.334  1.00 14.51           C  
ANISOU 1912  C   TYR A 250     1882   1830   1801    116    -18    -58       C  
ATOM   1913  O   TYR A 250      31.234  53.934  74.028  1.00 14.97           O  
ANISOU 1913  O   TYR A 250     1925   1893   1870    120    -15    -46       O  
ATOM   1914  CB  TYR A 250      33.858  56.127  73.672  1.00 14.49           C  
ANISOU 1914  CB  TYR A 250     1889   1820   1795     87    -35    -77       C  
ATOM   1915  CG  TYR A 250      34.573  54.831  73.777  1.00 13.46           C  
ANISOU 1915  CG  TYR A 250     1741   1704   1670     84    -41    -69       C  
ATOM   1916  CD1 TYR A 250      34.435  54.047  74.906  1.00 14.16           C  
ANISOU 1916  CD1 TYR A 250     1824   1805   1750     92    -40    -62       C  
ATOM   1917  CD2 TYR A 250      35.377  54.386  72.755  1.00 13.29           C  
ANISOU 1917  CD2 TYR A 250     1707   1682   1660     73    -47    -67       C  
ATOM   1918  CE1 TYR A 250      35.113  52.856  75.013  1.00 14.21           C  
ANISOU 1918  CE1 TYR A 250     1815   1823   1761     90    -45    -53       C  
ATOM   1919  CE2 TYR A 250      36.045  53.167  72.827  1.00 13.65           C  
ANISOU 1919  CE2 TYR A 250     1737   1740   1712     72    -51    -59       C  
ATOM   1920  CZ  TYR A 250      35.899  52.394  73.960  1.00 13.49           C  
ANISOU 1920  CZ  TYR A 250     1712   1730   1684     81    -50    -52       C  
ATOM   1921  OH  TYR A 250      36.550  51.220  74.047  1.00 14.29           O  
ANISOU 1921  OH  TYR A 250     1798   1841   1790     80    -54    -43       O  
ATOM   1922  N   LEU A 251      31.504  55.509  75.567  1.00 14.65           N  
ANISOU 1922  N   LEU A 251     1912   1852   1802    122    -15    -63       N  
ATOM   1923  CA  LEU A 251      30.888  54.694  76.603  1.00 13.96           C  
ANISOU 1923  CA  LEU A 251     1819   1777   1708    135     -9    -53       C  
ATOM   1924  C   LEU A 251      29.354  54.555  76.409  1.00 13.06           C  
ANISOU 1924  C   LEU A 251     1701   1661   1601    150      4    -43       C  
ATOM   1925  O   LEU A 251      28.743  53.521  76.737  1.00 13.05           O  
ANISOU 1925  O   LEU A 251     1687   1669   1604    157      9    -30       O  
ATOM   1926  CB  LEU A 251      31.193  55.358  77.978  1.00 15.38           C  
ANISOU 1926  CB  LEU A 251     2015   1964   1866    137    -10    -63       C  
ATOM   1927  CG  LEU A 251      30.633  54.620  79.171  1.00 16.56           C  
ANISOU 1927  CG  LEU A 251     2161   2128   2005    149     -4    -53       C  
ATOM   1928  CD1 LEU A 251      31.201  53.222  79.282  1.00 17.39           C  
ANISOU 1928  CD1 LEU A 251     2246   2245   2115    146    -10    -40       C  
ATOM   1929  CD2 LEU A 251      30.883  55.441  80.434  1.00 18.19           C  
ANISOU 1929  CD2 LEU A 251     2385   2339   2187    152     -4    -65       C  
ATOM   1930  N   ASP A 252      28.754  55.623  75.882  1.00 12.12           N  
ANISOU 1930  N   ASP A 252     1592   1529   1483    154      9    -49       N  
ATOM   1931  CA  ASP A 252      27.342  55.613  75.538  1.00 11.65           C  
ANISOU 1931  CA  ASP A 252     1528   1467   1431    168     20    -40       C  
ATOM   1932  C   ASP A 252      27.025  54.451  74.617  1.00 11.32           C  
ANISOU 1932  C   ASP A 252     1465   1430   1407    164     19    -27       C  
ATOM   1933  O   ASP A 252      25.936  53.901  74.691  1.00 10.97           O  
ANISOU 1933  O   ASP A 252     1410   1390   1368    174     27    -15       O  
ATOM   1934  CB  ASP A 252      26.942  56.916  74.839  1.00 12.42           C  
ANISOU 1934  CB  ASP A 252     1639   1550   1531    171     23    -48       C  
ATOM   1935  CG  ASP A 252      25.439  57.146  74.822  1.00 12.37           C  
ANISOU 1935  CG  ASP A 252     1630   1543   1527    190     36    -40       C  
ATOM   1936  OD1 ASP A 252      24.740  56.867  75.838  1.00 14.41           O  
ANISOU 1936  OD1 ASP A 252     1887   1811   1776    202     45    -34       O  
ATOM   1937  OD2 ASP A 252      24.916  57.598  73.750  1.00 14.95           O  
ANISOU 1937  OD2 ASP A 252     1955   1861   1864    192     38    -37       O  
ATOM   1938  N   GLN A 253      27.966  54.087  73.734  1.00 10.59           N  
ANISOU 1938  N   GLN A 253     1366   1333   1324    150      9    -29       N  
ATOM   1939  CA  GLN A 253      27.719  52.937  72.829  1.00 10.33           C  
ANISOU 1939  CA  GLN A 253     1315   1303   1308    146      8    -19       C  
ATOM   1940  C   GLN A 253      27.505  51.666  73.627  1.00 10.10           C  
ANISOU 1940  C   GLN A 253     1273   1285   1279    150     10     -7       C  
ATOM   1941  O   GLN A 253      26.574  50.944  73.346  1.00  9.69           O  
ANISOU 1941  O   GLN A 253     1210   1236   1237    154     16      4       O  
ATOM   1942  CB  GLN A 253      28.889  52.794  71.892  1.00 10.16           C  
ANISOU 1942  CB  GLN A 253     1291   1277   1294    131     -3    -24       C  
ATOM   1943  CG  GLN A 253      28.669  51.734  70.810  1.00  9.57           C  
ANISOU 1943  CG  GLN A 253     1199   1202   1235    126     -4    -16       C  
ATOM   1944  CD  GLN A 253      27.556  52.163  69.898  1.00  9.43           C  
ANISOU 1944  CD  GLN A 253     1180   1179   1225    130      1    -13       C  
ATOM   1945  OE1 GLN A 253      27.382  53.351  69.624  1.00 10.48           O  
ANISOU 1945  OE1 GLN A 253     1324   1304   1353    133      2    -19       O  
ATOM   1946  NE2 GLN A 253      26.768  51.198  69.438  1.00  8.86           N  
ANISOU 1946  NE2 GLN A 253     1093   1110   1163    132      4     -3       N  
ATOM   1947  N   LEU A 254      28.374  51.382  74.586  1.00 11.26           N  
ANISOU 1947  N   LEU A 254     1423   1439   1416    147      6     -9       N  
ATOM   1948  CA  LEU A 254      28.172  50.211  75.457  1.00 11.08           C  
ANISOU 1948  CA  LEU A 254     1390   1427   1392    152      9      4       C  
ATOM   1949  C   LEU A 254      26.855  50.294  76.197  1.00 11.10           C  
ANISOU 1949  C   LEU A 254     1394   1436   1389    167     22     12       C  
ATOM   1950  O   LEU A 254      26.127  49.314  76.287  1.00 11.28           O  
ANISOU 1950  O   LEU A 254     1404   1463   1420    170     27     26       O  
ATOM   1951  CB  LEU A 254      29.340  50.129  76.415  1.00 11.98           C  
ANISOU 1951  CB  LEU A 254     1509   1549   1492    149      2      0       C  
ATOM   1952  CG  LEU A 254      29.250  49.003  77.474  1.00 12.18           C  
ANISOU 1952  CG  LEU A 254     1527   1586   1513    155      5     14       C  
ATOM   1953  CD1 LEU A 254      29.241  47.630  76.762  1.00 12.50           C  
ANISOU 1953  CD1 LEU A 254     1551   1625   1574    151      5     26       C  
ATOM   1954  CD2 LEU A 254      30.375  49.114  78.488  1.00 12.46           C  
ANISOU 1954  CD2 LEU A 254     1569   1632   1533    153     -2      9       C  
ATOM   1955  N   ASN A 255      26.504  51.465  76.684  1.00 11.57           N  
ANISOU 1955  N   ASN A 255     1468   1493   1435    174     26      4       N  
ATOM   1956  CA  ASN A 255      25.278  51.617  77.442  1.00 11.90           C  
ANISOU 1956  CA  ASN A 255     1511   1542   1470    190     39     11       C  
ATOM   1957  C   ASN A 255      24.024  51.365  76.578  1.00 11.55           C  
ANISOU 1957  C   ASN A 255     1453   1494   1441    194     46     21       C  
ATOM   1958  O   ASN A 255      23.041  50.758  77.009  1.00 10.98           O  
ANISOU 1958  O   ASN A 255     1370   1431   1370    202     56     34       O  
ATOM   1959  CB  ASN A 255      25.239  52.986  78.111  1.00 12.32           C  
ANISOU 1959  CB  ASN A 255     1584   1592   1506    198     43     -3       C  
ATOM   1960  CG  ASN A 255      26.271  53.121  79.223  1.00 13.12           C  
ANISOU 1960  CG  ASN A 255     1696   1700   1588    194     37    -11       C  
ATOM   1961  OD1 ASN A 255      26.751  52.097  79.784  1.00 13.93           O  
ANISOU 1961  OD1 ASN A 255     1790   1813   1689    191     33     -2       O  
ATOM   1962  ND2 ASN A 255      26.623  54.326  79.550  1.00 14.03           N  
ANISOU 1962  ND2 ASN A 255     1831   1809   1691    194     36    -26       N  
ATOM   1963  N   HIS A 256      24.069  51.828  75.323  1.00 10.79           N  
ANISOU 1963  N   HIS A 256     1357   1388   1356    188     42     15       N  
ATOM   1964  CA  HIS A 256      23.017  51.516  74.366  1.00 10.62           C  
ANISOU 1964  CA  HIS A 256     1321   1364   1348    190     45     24       C  
ATOM   1965  C   HIS A 256      22.804  50.009  74.229  1.00 10.19           C  
ANISOU 1965  C   HIS A 256     1248   1316   1306    183     45     38       C  
ATOM   1966  O   HIS A 256      21.683  49.496  74.207  1.00 10.76           O  
ANISOU 1966  O   HIS A 256     1308   1395   1385    188     52     50       O  
ATOM   1967  CB  HIS A 256      23.313  52.142  72.992  1.00 11.14           C  
ANISOU 1967  CB  HIS A 256     1390   1419   1424    182     38     16       C  
ATOM   1968  CG  HIS A 256      22.764  53.527  72.858  1.00 11.80           C  
ANISOU 1968  CG  HIS A 256     1486   1496   1501    193     44     10       C  
ATOM   1969  ND1 HIS A 256      21.603  53.763  72.167  1.00 14.08           N  
ANISOU 1969  ND1 HIS A 256     1766   1785   1798    200     49     18       N  
ATOM   1970  CD2 HIS A 256      23.153  54.718  73.377  1.00 12.38           C  
ANISOU 1970  CD2 HIS A 256     1579   1563   1562    197     45     -2       C  
ATOM   1971  CE1 HIS A 256      21.322  55.051  72.229  1.00 14.49           C  
ANISOU 1971  CE1 HIS A 256     1833   1830   1842    211     54     11       C  
ATOM   1972  NE2 HIS A 256      22.272  55.653  72.914  1.00 13.77           N  
ANISOU 1972  NE2 HIS A 256     1760   1734   1740    209     51     -1       N  
ATOM   1973  N   ILE A 257      23.932  49.302  74.088  1.00  9.63           N  
ANISOU 1973  N   ILE A 257     1175   1243   1239    172     36     35       N  
ATOM   1974  CA  ILE A 257      23.885  47.854  73.860  1.00  9.66           C  
ANISOU 1974  CA  ILE A 257     1165   1250   1257    165     35     46       C  
ATOM   1975  C   ILE A 257      23.260  47.173  75.051  1.00 10.71           C  
ANISOU 1975  C   ILE A 257     1292   1392   1384    173     44     60       C  
ATOM   1976  O   ILE A 257      22.365  46.318  74.894  1.00  9.67           O  
ANISOU 1976  O   ILE A 257     1147   1264   1264    172     49     72       O  
ATOM   1977  CB  ILE A 257      25.265  47.306  73.548  1.00  9.91           C  
ANISOU 1977  CB  ILE A 257     1197   1277   1292    153     24     41       C  
ATOM   1978  CG1 ILE A 257      25.750  47.850  72.172  1.00  9.68           C  
ANISOU 1978  CG1 ILE A 257     1170   1238   1270    144     17     30       C  
ATOM   1979  CG2 ILE A 257      25.226  45.786  73.516  1.00 10.15           C  
ANISOU 1979  CG2 ILE A 257     1214   1308   1335    148     25     53       C  
ATOM   1980  CD1 ILE A 257      27.212  47.665  71.893  1.00 10.05           C  
ANISOU 1980  CD1 ILE A 257     1219   1281   1317    134      7     22       C  
ATOM   1981  N   LEU A 258      23.728  47.571  76.245  1.00 10.72           N  
ANISOU 1981  N   LEU A 258     1304   1401   1369    180     45     57       N  
ATOM   1982  CA  LEU A 258      23.281  46.957  77.494  1.00 11.77           C  
ANISOU 1982  CA  LEU A 258     1433   1544   1493    188     54     70       C  
ATOM   1983  C   LEU A 258      21.809  47.284  77.778  1.00 12.01           C  
ANISOU 1983  C   LEU A 258     1459   1581   1521    199     67     78       C  
ATOM   1984  O   LEU A 258      21.103  46.514  78.378  1.00 12.42           O  
ANISOU 1984  O   LEU A 258     1502   1642   1575    203     75     92       O  
ATOM   1985  CB  LEU A 258      24.178  47.394  78.625  1.00 12.46           C  
ANISOU 1985  CB  LEU A 258     1535   1639   1561    192     51     63       C  
ATOM   1986  CG  LEU A 258      25.600  46.832  78.573  1.00 13.78           C  
ANISOU 1986  CG  LEU A 258     1703   1804   1730    181     39     60       C  
ATOM   1987  CD1 LEU A 258      26.384  47.476  79.683  1.00 15.06           C  
ANISOU 1987  CD1 LEU A 258     1879   1974   1870    185     36     52       C  
ATOM   1988  CD2 LEU A 258      25.652  45.316  78.648  1.00 15.16           C  
ANISOU 1988  CD2 LEU A 258     1863   1980   1916    178     39     76       C  
ATOM   1989  N   GLY A 259      21.346  48.420  77.272  1.00 11.83           N  
ANISOU 1989  N   GLY A 259     1443   1555   1498    205     69     69       N  
ATOM   1990  CA  GLY A 259      19.921  48.795  77.412  1.00 12.57           C  
ANISOU 1990  CA  GLY A 259     1530   1654   1590    217     81     76       C  
ATOM   1991  C   GLY A 259      18.956  47.850  76.701  1.00 12.65           C  
ANISOU 1991  C   GLY A 259     1520   1667   1619    212     84     91       C  
ATOM   1992  O   GLY A 259      17.758  47.684  77.116  1.00 13.17           O  
ANISOU 1992  O   GLY A 259     1575   1743   1685    221     96    103       O  
ATOM   1993  N   ILE A 260      19.434  47.189  75.649  1.00 11.53           N  
ANISOU 1993  N   ILE A 260     1371   1517   1492    197     74     89       N  
ATOM   1994  CA  ILE A 260      18.618  46.237  74.944  1.00 11.69           C  
ANISOU 1994  CA  ILE A 260     1373   1539   1530    189     75    101       C  
ATOM   1995  C   ILE A 260      18.924  44.801  75.312  1.00 11.30           C  
ANISOU 1995  C   ILE A 260     1316   1489   1488    180     74    111       C  
ATOM   1996  O   ILE A 260      18.023  44.040  75.633  1.00 10.94           O  
ANISOU 1996  O   ILE A 260     1258   1451   1449    180     82    126       O  
ATOM   1997  CB  ILE A 260      18.715  46.460  73.415  1.00 12.20           C  
ANISOU 1997  CB  ILE A 260     1435   1594   1607    180     65     93       C  
ATOM   1998  CG1 ILE A 260      17.928  47.723  73.026  1.00 13.47           C  
ANISOU 1998  CG1 ILE A 260     1598   1757   1764    191     69     89       C  
ATOM   1999  CG2 ILE A 260      18.238  45.218  72.672  1.00 12.18           C  
ANISOU 1999  CG2 ILE A 260     1415   1590   1621    166     63    102       C  
ATOM   2000  CD1 ILE A 260      18.145  48.263  71.623  1.00 14.13           C  
ANISOU 2000  CD1 ILE A 260     1683   1832   1854    184     60     80       C  
ATOM   2001  N   LEU A 261      20.195  44.460  75.412  1.00 10.87           N  
ANISOU 2001  N   LEU A 261     1270   1429   1433    174     66    105       N  
ATOM   2002  CA  LEU A 261      20.572  43.110  75.757  1.00 11.48           C  
ANISOU 2002  CA  LEU A 261     1341   1505   1517    167     65    115       C  
ATOM   2003  C   LEU A 261      20.365  42.769  77.211  1.00 11.39           C  
ANISOU 2003  C   LEU A 261     1330   1504   1494    176     75    128       C  
ATOM   2004  O   LEU A 261      20.260  41.572  77.547  1.00 11.24           O  
ANISOU 2004  O   LEU A 261     1303   1485   1483    172     78    142       O  
ATOM   2005  CB  LEU A 261      22.011  42.838  75.399  1.00 11.65           C  
ANISOU 2005  CB  LEU A 261     1369   1517   1540    159     54    106       C  
ATOM   2006  CG  LEU A 261      22.373  42.780  73.931  1.00 12.62           C  
ANISOU 2006  CG  LEU A 261     1490   1629   1677    148     45     96       C  
ATOM   2007  CD1 LEU A 261      23.798  42.249  73.781  1.00 12.75           C  
ANISOU 2007  CD1 LEU A 261     1511   1638   1696    141     37     90       C  
ATOM   2008  CD2 LEU A 261      21.367  42.021  73.146  1.00 14.45           C  
ANISOU 2008  CD2 LEU A 261     1707   1857   1925    140     48    103       C  
ATOM   2009  N   GLY A 262      20.327  43.805  78.040  1.00 11.20           N  
ANISOU 2009  N   GLY A 262     1316   1487   1450    189     79    123       N  
ATOM   2010  CA  GLY A 262      20.179  43.651  79.497  1.00 11.79           C  
ANISOU 2010  CA  GLY A 262     1395   1576   1511    199     88    133       C  
ATOM   2011  C   GLY A 262      21.499  43.341  80.168  1.00 11.26           C  
ANISOU 2011  C   GLY A 262     1336   1508   1433    198     81    131       C  
ATOM   2012  O   GLY A 262      22.558  43.314  79.538  1.00 11.54           O  
ANISOU 2012  O   GLY A 262     1377   1535   1474    189     69    121       O  
ATOM   2013  N   SER A 263      21.438  43.111  81.482  1.00 11.13           N  
ANISOU 2013  N   SER A 263     1323   1504   1402    206     88    141       N  
ATOM   2014  CA  SER A 263      22.626  42.802  82.279  1.00 11.07           C  
ANISOU 2014  CA  SER A 263     1323   1500   1382    207     81    141       C  
ATOM   2015  C   SER A 263      23.256  41.492  81.832  1.00 11.46           C  
ANISOU 2015  C   SER A 263     1364   1541   1449    196     75    150       C  
ATOM   2016  O   SER A 263      22.581  40.452  81.714  1.00 12.50           O  
ANISOU 2016  O   SER A 263     1484   1670   1596    193     81    166       O  
ATOM   2017  CB  SER A 263      22.207  42.656  83.741  1.00 11.71           C  
ANISOU 2017  CB  SER A 263     1406   1597   1444    218     92    154       C  
ATOM   2018  OG  SER A 263      21.564  43.831  84.151  1.00 12.43           O  
ANISOU 2018  OG  SER A 263     1506   1696   1520    229     99    145       O  
ATOM   2019  N   PRO A 264      24.569  41.480  81.643  1.00 11.82           N  
ANISOU 2019  N   PRO A 264     1415   1582   1493    192     63    141       N  
ATOM   2020  CA  PRO A 264      25.213  40.197  81.366  1.00 11.90           C  
ANISOU 2020  CA  PRO A 264     1418   1585   1518    185     58    151       C  
ATOM   2021  C   PRO A 264      24.990  39.192  82.471  1.00 12.29           C  
ANISOU 2021  C   PRO A 264     1463   1642   1564    191     65    173       C  
ATOM   2022  O   PRO A 264      25.008  39.553  83.636  1.00 13.07           O  
ANISOU 2022  O   PRO A 264     1568   1756   1642    200     69    177       O  
ATOM   2023  CB  PRO A 264      26.710  40.583  81.207  1.00 11.85           C  
ANISOU 2023  CB  PRO A 264     1419   1578   1506    182     44    138       C  
ATOM   2024  CG  PRO A 264      26.666  41.997  80.724  1.00 12.22           C  
ANISOU 2024  CG  PRO A 264     1474   1623   1545    181     41    118       C  
ATOM   2025  CD  PRO A 264      25.475  42.604  81.423  1.00 12.44           C  
ANISOU 2025  CD  PRO A 264     1505   1660   1561    190     53    121       C  
ATOM   2026  N   SER A 265      24.821  37.939  82.072  1.00 12.55           N  
ANISOU 2026  N   SER A 265     1486   1665   1617    185     68    186       N  
ATOM   2027  CA  SER A 265      24.731  36.847  83.002  1.00 13.17           C  
ANISOU 2027  CA  SER A 265     1561   1748   1696    189     74    209       C  
ATOM   2028  C   SER A 265      26.000  36.696  83.798  1.00 13.39           C  
ANISOU 2028  C   SER A 265     1596   1784   1710    195     67    211       C  
ATOM   2029  O   SER A 265      27.082  37.117  83.363  1.00 13.17           O  
ANISOU 2029  O   SER A 265     1571   1753   1679    192     55    197       O  
ATOM   2030  CB  SER A 265      24.453  35.545  82.262  1.00 12.83           C  
ANISOU 2030  CB  SER A 265     1509   1688   1679    179     77    220       C  
ATOM   2031  OG  SER A 265      25.558  35.120  81.455  1.00 13.43           O  
ANISOU 2031  OG  SER A 265     1585   1750   1766    174     66    211       O  
ATOM   2032  N   GLN A 266      25.912  35.942  84.904  1.00 13.94           N  
ANISOU 2032  N   GLN A 266     1663   1861   1771    202     73    232       N  
ATOM   2033  CA  GLN A 266      27.117  35.614  85.684  1.00 15.27           C  
ANISOU 2033  CA  GLN A 266     1836   2039   1928    208     65    238       C  
ATOM   2034  C   GLN A 266      28.178  34.876  84.874  1.00 13.72           C  
ANISOU 2034  C   GLN A 266     1635   1827   1749    203     56    237       C  
ATOM   2035  O   GLN A 266      29.394  35.165  84.994  1.00 13.04           O  
ANISOU 2035  O   GLN A 266     1553   1748   1654    205     44    229       O  
ATOM   2036  CB  GLN A 266      26.744  34.832  86.943  1.00 16.84           C  
ANISOU 2036  CB  GLN A 266     2033   2249   2118    216     75    264       C  
ATOM   2037  CG  GLN A 266      27.889  34.707  87.936  1.00 18.62           C  
ANISOU 2037  CG  GLN A 266     2263   2489   2324    225     67    271       C  
ATOM   2038  CD  GLN A 266      28.328  36.061  88.455  1.00 19.76           C  
ANISOU 2038  CD  GLN A 266     2417   2650   2440    229     59    252       C  
ATOM   2039  OE1 GLN A 266      27.540  36.793  89.042  1.00 22.10           O  
ANISOU 2039  OE1 GLN A 266     2718   2958   2720    233     67    249       O  
ATOM   2040  NE2 GLN A 266      29.604  36.444  88.170  1.00 20.85           N  
ANISOU 2040  NE2 GLN A 266     2558   2790   2574    227     44    238       N  
ATOM   2041  N   GLU A 267      27.778  33.927  84.028  1.00 12.39           N  
ANISOU 2041  N   GLU A 267     1461   1641   1607    196     60    243       N  
ATOM   2042  CA  GLU A 267      28.743  33.203  83.202  1.00 13.59           C  
ANISOU 2042  CA  GLU A 267     1611   1777   1777    192     53    240       C  
ATOM   2043  C   GLU A 267      29.454  34.164  82.263  1.00 12.99           C  
ANISOU 2043  C   GLU A 267     1536   1699   1699    187     42    215       C  
ATOM   2044  O   GLU A 267      30.651  34.080  82.092  1.00 12.81           O  
ANISOU 2044  O   GLU A 267     1514   1676   1677    188     32    210       O  
ATOM   2045  CB  GLU A 267      28.075  32.070  82.393  1.00 15.42           C  
ANISOU 2045  CB  GLU A 267     1836   1987   2036    183     60    248       C  
ATOM   2046  CG  GLU A 267      29.013  31.401  81.418  1.00 17.95           C  
ANISOU 2046  CG  GLU A 267     2155   2290   2375    180     53    242       C  
ATOM   2047  CD  GLU A 267      28.351  30.255  80.692  1.00 22.96           C  
ANISOU 2047  CD  GLU A 267     2785   2902   3035    171     61    250       C  
ATOM   2048  OE1 GLU A 267      28.174  29.193  81.311  1.00 30.04           O  
ANISOU 2048  OE1 GLU A 267     3682   3794   3940    174     68    271       O  
ATOM   2049  OE2 GLU A 267      28.109  30.384  79.496  1.00 26.78           O  
ANISOU 2049  OE2 GLU A 267     3268   3374   3532    161     59    234       O  
ATOM   2050  N   ASP A 268      28.716  35.100  81.678  1.00 12.65           N  
ANISOU 2050  N   ASP A 268     1496   1656   1656    181     43    200       N  
ATOM   2051  CA  ASP A 268      29.320  36.056  80.760  1.00 12.44           C  
ANISOU 2051  CA  ASP A 268     1473   1627   1629    175     33    177       C  
ATOM   2052  C   ASP A 268      30.220  37.002  81.508  1.00 12.17           C  
ANISOU 2052  C   ASP A 268     1444   1608   1571    181     25    169       C  
ATOM   2053  O   ASP A 268      31.331  37.319  80.997  1.00 12.36           O  
ANISOU 2053  O   ASP A 268     1469   1631   1595    177     15    157       O  
ATOM   2054  CB  ASP A 268      28.239  36.799  79.923  1.00 12.51           C  
ANISOU 2054  CB  ASP A 268     1482   1630   1643    169     37    165       C  
ATOM   2055  CG  ASP A 268      27.608  35.884  78.832  1.00 12.86           C  
ANISOU 2055  CG  ASP A 268     1518   1656   1712    159     41    168       C  
ATOM   2056  OD1 ASP A 268      28.023  34.696  78.605  1.00 14.63           O  
ANISOU 2056  OD1 ASP A 268     1738   1869   1951    157     42    177       O  
ATOM   2057  OD2 ASP A 268      26.662  36.388  78.150  1.00 14.87           O  
ANISOU 2057  OD2 ASP A 268     1771   1908   1972    154     44    161       O  
ATOM   2058  N   LEU A 269      29.831  37.417  82.712  1.00 11.84           N  
ANISOU 2058  N   LEU A 269     1408   1583   1509    188     29    175       N  
ATOM   2059  CA  LEU A 269      30.702  38.244  83.546  1.00 12.94           C  
ANISOU 2059  CA  LEU A 269     1555   1739   1624    193     21    168       C  
ATOM   2060  C   LEU A 269      31.987  37.512  83.917  1.00 12.96           C  
ANISOU 2060  C   LEU A 269     1553   1746   1625    196     12    177       C  
ATOM   2061  O   LEU A 269      33.071  38.118  83.968  1.00 12.99           O  
ANISOU 2061  O   LEU A 269     1560   1759   1619    194      0    165       O  
ATOM   2062  CB  LEU A 269      30.014  38.676  84.815  1.00 13.09           C  
ANISOU 2062  CB  LEU A 269     1580   1774   1621    201     28    174       C  
ATOM   2063  CG  LEU A 269      28.864  39.679  84.687  1.00 14.16           C  
ANISOU 2063  CG  LEU A 269     1721   1910   1751    201     36    164       C  
ATOM   2064  CD1 LEU A 269      28.160  39.871  86.049  1.00 14.60           C  
ANISOU 2064  CD1 LEU A 269     1781   1982   1784    212     45    174       C  
ATOM   2065  CD2 LEU A 269      29.393  40.984  84.120  1.00 13.75           C  
ANISOU 2065  CD2 LEU A 269     1676   1855   1691    196     27    139       C  
ATOM   2066  N   ASN A 270      31.887  36.205  84.175  1.00 12.64           N  
ANISOU 2066  N   ASN A 270     1506   1701   1597    201     17    198       N  
ATOM   2067  CA  ASN A 270      33.073  35.419  84.530  1.00 13.36           C  
ANISOU 2067  CA  ASN A 270     1593   1796   1688    206     10    209       C  
ATOM   2068  C   ASN A 270      34.047  35.221  83.407  1.00 13.83           C  
ANISOU 2068  C   ASN A 270     1647   1844   1764    201      2    198       C  
ATOM   2069  O   ASN A 270      35.163  34.766  83.665  1.00 15.03           O  
ANISOU 2069  O   ASN A 270     1795   2003   1915    206     -6    205       O  
ATOM   2070  CB  ASN A 270      32.632  34.081  85.160  1.00 13.44           C  
ANISOU 2070  CB  ASN A 270     1599   1803   1706    213     20    236       C  
ATOM   2071  CG  ASN A 270      32.066  34.240  86.547  1.00 14.13           C  
ANISOU 2071  CG  ASN A 270     1689   1908   1770    221     25    249       C  
ATOM   2072  OD1 ASN A 270      32.256  35.256  87.217  1.00 16.34           O  
ANISOU 2072  OD1 ASN A 270     1976   2206   2025    223     20    239       O  
ATOM   2073  ND2 ASN A 270      31.361  33.259  86.996  1.00 14.16           N  
ANISOU 2073  ND2 ASN A 270     1691   1909   1782    225     36    271       N  
ATOM   2074  N   CYS A 271      33.687  35.605  82.192  1.00 13.75           N  
ANISOU 2074  N   CYS A 271     1637   1819   1767    191      3    182       N  
ATOM   2075  CA  CYS A 271      34.604  35.591  81.037  1.00 13.82           C  
ANISOU 2075  CA  CYS A 271     1641   1818   1790    185     -4    170       C  
ATOM   2076  C   CYS A 271      35.312  36.983  80.885  1.00 12.73           C  
ANISOU 2076  C   CYS A 271     1508   1692   1637    180    -15    149       C  
ATOM   2077  O   CYS A 271      36.043  37.144  79.935  1.00 13.64           O  
ANISOU 2077  O   CYS A 271     1620   1801   1761    174    -21    137       O  
ATOM   2078  CB  CYS A 271      33.827  35.277  79.770  1.00 14.53           C  
ANISOU 2078  CB  CYS A 271     1731   1888   1903    177      2    163       C  
ATOM   2079  SG  CYS A 271      33.120  33.600  79.641  1.00 18.54           S  
ANISOU 2079  SG  CYS A 271     2234   2377   2434    180     14    184       S  
ATOM   2080  N   ILE A 272      35.057  37.903  81.804  1.00 12.95           N  
ANISOU 2080  N   ILE A 272     1544   1735   1643    181    -17    145       N  
ATOM   2081  CA  ILE A 272      35.629  39.285  81.787  1.00 13.44           C  
ANISOU 2081  CA  ILE A 272     1612   1807   1689    175    -26    126       C  
ATOM   2082  C   ILE A 272      36.402  39.450  83.069  1.00 12.59           C  
ANISOU 2082  C   ILE A 272     1506   1720   1558    180    -34    131       C  
ATOM   2083  O   ILE A 272      35.820  39.564  84.124  1.00 14.79           O  
ANISOU 2083  O   ILE A 272     1790   2009   1820    186    -30    138       O  
ATOM   2084  CB  ILE A 272      34.553  40.381  81.630  1.00 13.76           C  
ANISOU 2084  CB  ILE A 272     1662   1843   1722    171    -20    113       C  
ATOM   2085  CG1 ILE A 272      33.779  40.189  80.311  1.00 13.66           C  
ANISOU 2085  CG1 ILE A 272     1646   1811   1731    165    -14    108       C  
ATOM   2086  CG2 ILE A 272      35.177  41.797  81.594  1.00 14.40           C  
ANISOU 2086  CG2 ILE A 272     1751   1931   1788    164    -30     92       C  
ATOM   2087  CD1 ILE A 272      32.533  40.999  80.262  1.00 13.78           C  
ANISOU 2087  CD1 ILE A 272     1670   1824   1743    165     -6    102       C  
ATOM   2088  N   ILE A 273      37.722  39.411  82.982  1.00 11.74           N  
ANISOU 2088  N   ILE A 273     1391   1620   1448    178    -45    128       N  
ATOM   2089  CA AILE A 273      38.650  39.473  84.124  0.30 11.37           C  
ANISOU 2089  CA AILE A 273     1344   1596   1381    183    -55    134       C  
ATOM   2090  CA BILE A 273      38.520  39.539  84.226  0.70 11.44           C  
ANISOU 2090  CA BILE A 273     1353   1605   1388    183    -55    134       C  
ATOM   2091  C   ILE A 273      39.176  40.909  84.400  1.00 11.24           C  
ANISOU 2091  C   ILE A 273     1334   1592   1343    173    -66    114       C  
ATOM   2092  O   ILE A 273      39.674  41.222  85.478  1.00 10.79           O  
ANISOU 2092  O   ILE A 273     1280   1555   1264    175    -74    116       O  
ATOM   2093  CB AILE A 273      39.841  38.540  83.817  0.30 11.46           C  
ANISOU 2093  CB AILE A 273     1341   1609   1405    186    -62    145       C  
ATOM   2094  CB BILE A 273      39.531  38.366  84.434  0.70 11.76           C  
ANISOU 2094  CB BILE A 273     1381   1652   1435    191    -60    152       C  
ATOM   2095  CG1AILE A 273      39.360  37.101  83.589  0.30 11.49           C  
ANISOU 2095  CG1AILE A 273     1338   1598   1429    196    -51    164       C  
ATOM   2096  CG1BILE A 273      40.749  38.521  83.531  0.70 12.21           C  
ANISOU 2096  CG1BILE A 273     1429   1709   1502    184    -70    142       C  
ATOM   2097  CG2AILE A 273      40.889  38.572  84.912  0.30 11.60           C  
ANISOU 2097  CG2AILE A 273     1354   1651   1401    191    -74    152       C  
ATOM   2098  CG2BILE A 273      38.870  36.979  84.203  0.70 11.96           C  
ANISOU 2098  CG2BILE A 273     1401   1661   1481    200    -47    172       C  
ATOM   2099  CD1AILE A 273      38.390  36.617  84.642  0.30 11.57           C  
ANISOU 2099  CD1AILE A 273     1353   1612   1430    205    -42    182       C  
ATOM   2100  CD1BILE A 273      41.838  37.517  83.854  0.70 12.33           C  
ANISOU 2100  CD1BILE A 273     1430   1733   1520    194    -76    159       C  
ATOM   2101  N   ASN A 274      39.064  41.790  83.394  1.00 10.07           N  
ANISOU 2101  N   ASN A 274     1191   1431   1202    162    -66     95       N  
ATOM   2102  CA  ASN A 274      39.453  43.198  83.550  1.00  9.99           C  
ANISOU 2102  CA  ASN A 274     1191   1428   1175    151    -75     75       C  
ATOM   2103  C   ASN A 274      38.651  43.801  84.702  1.00 10.44           C  
ANISOU 2103  C   ASN A 274     1262   1495   1209    156    -71     73       C  
ATOM   2104  O   ASN A 274      37.436  43.898  84.633  1.00  9.60           O  
ANISOU 2104  O   ASN A 274     1162   1378   1106    161    -59     74       O  
ATOM   2105  CB  ASN A 274      39.120  43.957  82.249  1.00  9.70           C  
ANISOU 2105  CB  ASN A 274     1159   1373   1152    141    -72     58       C  
ATOM   2106  CG  ASN A 274      40.150  43.754  81.169  1.00 10.12           C  
ANISOU 2106  CG  ASN A 274     1201   1421   1222    134    -78     54       C  
ATOM   2107  OD1 ASN A 274      41.292  43.294  81.418  1.00 11.14           O  
ANISOU 2107  OD1 ASN A 274     1320   1564   1350    134    -88     60       O  
ATOM   2108  ND2 ASN A 274      39.801  44.179  79.971  1.00 10.05           N  
ANISOU 2108  ND2 ASN A 274     1195   1396   1228    127    -74     43       N  
ATOM   2109  N   MET A 275      39.374  44.242  85.728  1.00 10.57           N  
ANISOU 2109  N   MET A 275     1282   1532   1203    154    -81     70       N  
ATOM   2110  CA AMET A 275      38.752  44.700  86.970  0.70 11.67           C  
ANISOU 2110  CA AMET A 275     1434   1683   1317    160    -78     69       C  
ATOM   2111  CA BMET A 275      38.780  44.715  86.967  0.30 11.64           C  
ANISOU 2111  CA BMET A 275     1430   1679   1313    160    -78     69       C  
ATOM   2112  C   MET A 275      37.866  45.918  86.693  1.00 11.35           C  
ANISOU 2112  C   MET A 275     1410   1630   1272    156    -71     50       C  
ATOM   2113  O   MET A 275      36.753  46.016  87.219  1.00 11.47           O  
ANISOU 2113  O   MET A 275     1434   1644   1279    165    -59     53       O  
ATOM   2114  CB AMET A 275      39.802  45.078  88.006  0.70 12.76           C  
ANISOU 2114  CB AMET A 275     1573   1845   1429    156    -93     66       C  
ATOM   2115  CB BMET A 275      39.906  45.102  87.932  0.30 12.69           C  
ANISOU 2115  CB BMET A 275     1564   1836   1421    155    -94     65       C  
ATOM   2116  CG AMET A 275      39.176  45.556  89.301  0.70 14.20           C  
ANISOU 2116  CG AMET A 275     1771   2041   1583    162    -89     64       C  
ATOM   2117  CG BMET A 275      39.445  45.583  89.282  0.30 13.86           C  
ANISOU 2117  CG BMET A 275     1726   2000   1540    160    -93     63       C  
ATOM   2118  SD AMET A 275      40.369  46.420  90.324  0.70 15.84           S  
ANISOU 2118  SD AMET A 275     1985   2274   1759    152   -108     50       S  
ATOM   2119  SD BMET A 275      39.271  47.367  89.367  0.30 15.51           S  
ANISOU 2119  SD BMET A 275     1957   2204   1730    148    -95     32       S  
ATOM   2120  CE AMET A 275      40.509  48.006  89.475  0.70 15.94           C  
ANISOU 2120  CE AMET A 275     2011   2270   1774    134   -112     18       C  
ATOM   2121  CE BMET A 275      40.950  47.962  89.151  0.30 15.29           C  
ANISOU 2121  CE BMET A 275     1924   2187   1698    129   -117     17       C  
ATOM   2122  N   LYS A 276      38.372  46.854  85.910  1.00 11.12           N  
ANISOU 2122  N   LYS A 276     1386   1593   1248    143    -78     31       N  
ATOM   2123  CA  LYS A 276      37.585  48.086  85.659  1.00 11.46           C  
ANISOU 2123  CA  LYS A 276     1446   1623   1287    139    -71     13       C  
ATOM   2124  C   LYS A 276      36.317  47.788  84.853  1.00 10.50           C  
ANISOU 2124  C   LYS A 276     1323   1482   1185    146    -56     19       C  
ATOM   2125  O   LYS A 276      35.253  48.351  85.101  1.00 10.48           O  
ANISOU 2125  O   LYS A 276     1331   1474   1175    153    -46     15       O  
ATOM   2126  CB  LYS A 276      38.408  49.134  84.988  1.00 12.52           C  
ANISOU 2126  CB  LYS A 276     1586   1751   1422    123    -81     -7       C  
ATOM   2127  CG  LYS A 276      39.595  49.574  85.819  1.00 14.95           C  
ANISOU 2127  CG  LYS A 276     1895   2077   1708    113    -97    -15       C  
ATOM   2128  CD  LYS A 276      40.331  50.711  85.119  1.00 17.66           C  
ANISOU 2128  CD  LYS A 276     2245   2412   2054     95   -106    -35       C  
ATOM   2129  CE  LYS A 276      41.595  51.102  85.886  1.00 21.65           C  
ANISOU 2129  CE  LYS A 276     2750   2938   2539     83   -123    -43       C  
ATOM   2130  NZ  LYS A 276      42.326  52.253  85.249  1.00 25.16           N  
ANISOU 2130  NZ  LYS A 276     3201   3374   2986     63   -132    -63       N  
ATOM   2131  N   ALA A 277      36.428  46.940  83.858  1.00 10.30           N  
ANISOU 2131  N   ALA A 277     1284   1448   1184    145    -55     28       N  
ATOM   2132  CA  ALA A 277      35.254  46.523  83.109  1.00 10.00           C  
ANISOU 2132  CA  ALA A 277     1242   1394   1164    151    -42     35       C  
ATOM   2133  C   ALA A 277      34.240  45.834  83.984  1.00 10.26           C  
ANISOU 2133  C   ALA A 277     1274   1433   1191    164    -30     51       C  
ATOM   2134  O   ALA A 277      33.024  46.112  83.919  1.00 10.01           O  
ANISOU 2134  O   ALA A 277     1248   1395   1162    170    -19     52       O  
ATOM   2135  CB  ALA A 277      35.689  45.563  81.999  1.00  9.81           C  
ANISOU 2135  CB  ALA A 277     1203   1361   1165    147    -44     43       C  
ATOM   2136  N   ARG A 278      34.710  44.879  84.791  1.00 10.33           N  
ANISOU 2136  N   ARG A 278     1275   1455   1194    170    -33     67       N  
ATOM   2137  CA  ARG A 278      33.822  44.150  85.686  1.00 11.21           C  
ANISOU 2137  CA  ARG A 278     1385   1574   1300    182    -23     85       C  
ATOM   2138  C   ARG A 278      33.134  45.055  86.652  1.00 11.34           C  
ANISOU 2138  C   ARG A 278     1417   1600   1293    188    -17     78       C  
ATOM   2139  O   ARG A 278      31.925  44.957  86.857  1.00 11.51           O  
ANISOU 2139  O   ARG A 278     1439   1618   1315    196     -3     85       O  
ATOM   2140  CB  ARG A 278      34.580  43.035  86.427  1.00 12.14           C  
ANISOU 2140  CB  ARG A 278     1494   1705   1414    187    -28    104       C  
ATOM   2141  CG  ARG A 278      34.756  41.867  85.536  1.00 14.42           C  
ANISOU 2141  CG  ARG A 278     1769   1982   1730    186    -27    116       C  
ATOM   2142  CD  ARG A 278      33.489  40.953  85.542  1.00 15.10           C  
ANISOU 2142  CD  ARG A 278     1850   2058   1828    194    -11    134       C  
ATOM   2143  NE  ARG A 278      33.234  40.278  86.839  1.00 17.02           N  
ANISOU 2143  NE  ARG A 278     2093   2317   2057    204     -6    154       N  
ATOM   2144  CZ  ARG A 278      33.880  39.191  87.295  1.00 19.41           C  
ANISOU 2144  CZ  ARG A 278     2388   2626   2363    210    -10    172       C  
ATOM   2145  NH1 ARG A 278      34.832  38.576  86.578  1.00 18.01           N  
ANISOU 2145  NH1 ARG A 278     2200   2440   2201    207    -17    174       N  
ATOM   2146  NH2 ARG A 278      33.598  38.731  88.513  1.00 21.86           N  
ANISOU 2146  NH2 ARG A 278     2698   2950   2656    220     -5    190       N  
ATOM   2147  N   ASN A 279      33.897  45.932  87.311  1.00 11.68           N  
ANISOU 2147  N   ASN A 279     1470   1654   1313    184    -27     64       N  
ATOM   2148  CA  ASN A 279      33.308  46.795  88.306  1.00 12.61           C  
ANISOU 2148  CA  ASN A 279     1604   1781   1406    190    -21     56       C  
ATOM   2149  C   ASN A 279      32.319  47.760  87.642  1.00 11.89           C  
ANISOU 2149  C   ASN A 279     1522   1673   1322    190    -11     42       C  
ATOM   2150  O   ASN A 279      31.284  48.138  88.250  1.00 11.88           O  
ANISOU 2150  O   ASN A 279     1530   1675   1309    200      2     42       O  
ATOM   2151  CB  ASN A 279      34.375  47.560  89.059  1.00 14.23           C  
ANISOU 2151  CB  ASN A 279     1819   2001   1587    183    -35     41       C  
ATOM   2152  CG  ASN A 279      35.059  46.706  90.121  1.00 16.60           C  
ANISOU 2152  CG  ASN A 279     2112   2323   1872    187    -42     57       C  
ATOM   2153  OD1 ASN A 279      34.575  45.627  90.440  1.00 23.08           O  
ANISOU 2153  OD1 ASN A 279     2923   3148   2698    197    -34     79       O  
ATOM   2154  ND2 ASN A 279      36.253  47.133  90.566  1.00 17.09           N  
ANISOU 2154  ND2 ASN A 279     2176   2399   1917    178    -58     47       N  
ATOM   2155  N   TYR A 280      32.643  48.221  86.430  1.00 11.52           N  
ANISOU 2155  N   TYR A 280     1474   1610   1292    180    -16     30       N  
ATOM   2156  CA  TYR A 280      31.675  49.057  85.703  1.00 11.94           C  
ANISOU 2156  CA  TYR A 280     1536   1647   1354    181     -6     20       C  
ATOM   2157  C   TYR A 280      30.374  48.288  85.437  1.00 11.93           C  
ANISOU 2157  C   TYR A 280     1524   1641   1368    191      8     36       C  
ATOM   2158  O   TYR A 280      29.273  48.774  85.787  1.00 12.03           O  
ANISOU 2158  O   TYR A 280     1544   1654   1374    202     21     36       O  
ATOM   2159  CB  TYR A 280      32.242  49.589  84.416  1.00 11.92           C  
ANISOU 2159  CB  TYR A 280     1532   1629   1368    169    -14      7       C  
ATOM   2160  CG  TYR A 280      31.215  50.432  83.683  1.00 12.53           C  
ANISOU 2160  CG  TYR A 280     1617   1690   1453    172     -4     -2       C  
ATOM   2161  CD1 TYR A 280      30.885  51.693  84.149  1.00 12.89           C  
ANISOU 2161  CD1 TYR A 280     1682   1734   1483    175     -1    -17       C  
ATOM   2162  CD2 TYR A 280      30.558  49.956  82.573  1.00 12.10           C  
ANISOU 2162  CD2 TYR A 280     1551   1624   1422    172      1      6       C  
ATOM   2163  CE1 TYR A 280      29.944  52.462  83.506  1.00 13.17           C  
ANISOU 2163  CE1 TYR A 280     1724   1754   1525    180      9    -23       C  
ATOM   2164  CE2 TYR A 280      29.568  50.693  81.926  1.00 12.64           C  
ANISOU 2164  CE2 TYR A 280     1626   1680   1497    177     10      1       C  
ATOM   2165  CZ  TYR A 280      29.277  51.950  82.408  1.00 13.02           C  
ANISOU 2165  CZ  TYR A 280     1691   1725   1529    181     14    -14       C  
ATOM   2166  OH  TYR A 280      28.265  52.693  81.787  1.00 14.39           O  
ANISOU 2166  OH  TYR A 280     1870   1887   1710    188     24    -18       O  
ATOM   2167  N   LEU A 281      30.469  47.062  84.881  1.00 11.59           N  
ANISOU 2167  N   LEU A 281     1464   1595   1344    189      8     52       N  
ATOM   2168  CA  LEU A 281      29.263  46.322  84.559  1.00 11.77           C  
ANISOU 2168  CA  LEU A 281     1477   1612   1382    196     21     67       C  
ATOM   2169  C   LEU A 281      28.444  46.045  85.811  1.00 12.57           C  
ANISOU 2169  C   LEU A 281     1580   1728   1468    209     32     80       C  
ATOM   2170  O   LEU A 281      27.211  46.138  85.793  1.00 12.99           O  
ANISOU 2170  O   LEU A 281     1631   1779   1524    216     46     85       O  
ATOM   2171  CB  LEU A 281      29.621  45.032  83.855  1.00 11.70           C  
ANISOU 2171  CB  LEU A 281     1452   1597   1395    191     17     81       C  
ATOM   2172  CG  LEU A 281      30.173  45.221  82.444  1.00 11.15           C  
ANISOU 2172  CG  LEU A 281     1379   1513   1345    179      9     70       C  
ATOM   2173  CD1 LEU A 281      30.633  43.843  82.020  1.00 10.91           C  
ANISOU 2173  CD1 LEU A 281     1335   1479   1332    176      6     84       C  
ATOM   2174  CD2 LEU A 281      29.120  45.747  81.482  1.00 11.21           C  
ANISOU 2174  CD2 LEU A 281     1387   1508   1365    179     17     64       C  
ATOM   2175  N   GLN A 282      29.127  45.704  86.896  1.00 13.06           N  
ANISOU 2175  N   GLN A 282     1644   1805   1512    211     27     86       N  
ATOM   2176  CA  GLN A 282      28.427  45.352  88.144  1.00 15.26           C  
ANISOU 2176  CA  GLN A 282     1924   2100   1774    223     38    100       C  
ATOM   2177  C   GLN A 282      27.784  46.527  88.881  1.00 15.16           C  
ANISOU 2177  C   GLN A 282     1928   2094   1738    232     47     88       C  
ATOM   2178  O   GLN A 282      26.973  46.329  89.757  1.00 17.45           O  
ANISOU 2178  O   GLN A 282     2219   2396   2016    243     59     99       O  
ATOM   2179  CB  GLN A 282      29.387  44.519  89.016  1.00 17.17           C  
ANISOU 2179  CB  GLN A 282     2163   2357   2005    224     30    113       C  
ATOM   2180  CG  GLN A 282      29.633  43.159  88.335  1.00 19.83           C  
ANISOU 2180  CG  GLN A 282     2483   2685   2367    220     28    131       C  
ATOM   2181  CD  GLN A 282      30.715  42.253  88.914  1.00 22.94           C  
ANISOU 2181  CD  GLN A 282     2871   3090   2756    220     18    144       C  
ATOM   2182  OE1 GLN A 282      31.007  41.172  88.315  1.00 26.08           O  
ANISOU 2182  OE1 GLN A 282     3256   3478   3175    217     17    157       O  
ATOM   2183  NE2 GLN A 282      31.364  42.672  90.006  1.00 24.60           N  
ANISOU 2183  NE2 GLN A 282     3088   3319   2939    223     11    141       N  
ATOM   2184  N   SER A 283      28.049  47.727  88.436  1.00 14.87           N  
ANISOU 2184  N   SER A 283     1903   2048   1697    227     42     65       N  
ATOM   2185  CA  SER A 283      27.499  48.934  89.096  1.00 15.37           C  
ANISOU 2185  CA  SER A 283     1984   2115   1739    236     49     51       C  
ATOM   2186  C   SER A 283      26.169  49.307  88.472  1.00 15.99           C  
ANISOU 2186  C   SER A 283     2061   2183   1831    244     64     51       C  
ATOM   2187  O   SER A 283      25.465  50.185  88.936  1.00 18.15           O  
ANISOU 2187  O   SER A 283     2347   2458   2091    254     75     42       O  
ATOM   2188  CB  SER A 283      28.477  50.092  88.916  1.00 14.85           C  
ANISOU 2188  CB  SER A 283     1935   2044   1664    226     36     26       C  
ATOM   2189  OG  SER A 283      28.527  50.659  87.618  1.00 14.09           O  
ANISOU 2189  OG  SER A 283     1838   1927   1588    217     33     14       O  
ATOM   2190  N   LEU A 284      25.865  48.711  87.324  1.00 15.03           N  
ANISOU 2190  N   LEU A 284     1925   2049   1737    238     64     60       N  
ATOM   2191  CA  LEU A 284      24.714  49.192  86.518  1.00 15.68           C  
ANISOU 2191  CA  LEU A 284     2005   2120   1834    243     75     58       C  
ATOM   2192  C   LEU A 284      23.412  48.564  87.048  1.00 14.87           C  
ANISOU 2192  C   LEU A 284     1892   2028   1732    256     92     77       C  
ATOM   2193  O   LEU A 284      23.441  47.491  87.669  1.00 16.35           O  
ANISOU 2193  O   LEU A 284     2070   2226   1917    257     94     95       O  
ATOM   2194  CB  LEU A 284      24.913  48.798  85.048  1.00 15.05           C  
ANISOU 2194  CB  LEU A 284     1912   2024   1781    232     68     59       C  
ATOM   2195  CG  LEU A 284      26.168  49.387  84.371  1.00 15.36           C  
ANISOU 2195  CG  LEU A 284     1960   2054   1823    218     52     41       C  
ATOM   2196  CD1 LEU A 284      26.234  48.898  82.956  1.00 15.55           C  
ANISOU 2196  CD1 LEU A 284     1971   2064   1873    209     47     44       C  
ATOM   2197  CD2 LEU A 284      26.149  50.921  84.455  1.00 15.95           C  
ANISOU 2197  CD2 LEU A 284     2054   2122   1884    221     53     21       C  
ATOM   2198  N   PRO A 285      22.276  49.178  86.695  1.00 16.27           N  
ANISOU 2198  N   PRO A 285     2068   2200   1913    265    104     76       N  
ATOM   2199  CA  PRO A 285      21.021  48.608  87.209  1.00 16.67           C  
ANISOU 2199  CA  PRO A 285     2108   2262   1965    276    121     95       C  
ATOM   2200  C   PRO A 285      20.704  47.282  86.587  1.00 15.50           C  
ANISOU 2200  C   PRO A 285     1938   2112   1840    268    121    115       C  
ATOM   2201  O   PRO A 285      21.027  47.051  85.414  1.00 16.17           O  
ANISOU 2201  O   PRO A 285     2016   2183   1946    256    111    111       O  
ATOM   2202  CB  PRO A 285      19.953  49.651  86.806  1.00 17.17           C  
ANISOU 2202  CB  PRO A 285     2174   2320   2029    288    132     87       C  
ATOM   2203  CG  PRO A 285      20.687  50.938  86.590  1.00 18.18           C  
ANISOU 2203  CG  PRO A 285     2323   2436   2148    286    124     62       C  
ATOM   2204  CD  PRO A 285      22.121  50.575  86.208  1.00 16.60           C  
ANISOU 2204  CD  PRO A 285     2125   2230   1953    269    105     56       C  
ATOM   2205  N   SER A 286      20.157  46.374  87.363  1.00 15.98           N  
ANISOU 2205  N   SER A 286     1989   2186   1898    273    131    135       N  
ATOM   2206  CA ASER A 286      19.763  45.068  86.866  0.50 16.54           C  
ANISOU 2206  CA ASER A 286     2040   2254   1991    264    132    155       C  
ATOM   2207  CA BSER A 286      19.763  45.071  86.852  0.50 16.96           C  
ANISOU 2207  CA BSER A 286     2093   2307   2045    264    132    155       C  
ATOM   2208  C   SER A 286      18.649  45.236  85.818  1.00 16.21           C  
ANISOU 2208  C   SER A 286     1986   2205   1970    264    138    156       C  
ATOM   2209  O   SER A 286      17.678  45.947  86.038  1.00 18.48           O  
ANISOU 2209  O   SER A 286     2274   2499   2250    276    151    156       O  
ATOM   2210  CB ASER A 286      19.299  44.180  88.045  0.50 17.71           C  
ANISOU 2210  CB ASER A 286     2181   2418   2129    271    144    177       C  
ATOM   2211  CB BSER A 286      19.307  44.166  88.007  0.50 18.68           C  
ANISOU 2211  CB BSER A 286     2304   2541   2253    271    144    177       C  
ATOM   2212  OG ASER A 286      18.737  42.968  87.582  0.50 19.38           O  
ANISOU 2212  OG ASER A 286     2374   2626   2364    263    148    197       O  
ATOM   2213  OG BSER A 286      20.362  43.969  88.916  0.50 22.07           O  
ANISOU 2213  OG BSER A 286     2744   2978   2664    271    136    176       O  
ATOM   2214  N   LYS A 287      18.785  44.569  84.663  1.00 14.11           N  
ANISOU 2214  N   LYS A 287     1708   1925   1727    250    130    159       N  
ATOM   2215  CA  LYS A 287      17.784  44.704  83.583  1.00 13.98           C  
ANISOU 2215  CA  LYS A 287     1679   1902   1729    247    133    160       C  
ATOM   2216  C   LYS A 287      17.738  43.437  82.798  1.00 13.01           C  
ANISOU 2216  C   LYS A 287     1541   1772   1631    232    129    172       C  
ATOM   2217  O   LYS A 287      18.759  42.899  82.471  1.00 13.04           O  
ANISOU 2217  O   LYS A 287     1547   1767   1641    222    117    169       O  
ATOM   2218  CB  LYS A 287      18.121  45.861  82.623  1.00 14.27           C  
ANISOU 2218  CB  LYS A 287     1725   1927   1768    246    125    139       C  
ATOM   2219  CG  LYS A 287      17.002  46.109  81.611  1.00 15.30           C  
ANISOU 2219  CG  LYS A 287     1843   2055   1915    247    129    142       C  
ATOM   2220  CD  LYS A 287      17.206  47.382  80.798  1.00 16.46           C  
ANISOU 2220  CD  LYS A 287     2001   2192   2061    249    123    123       C  
ATOM   2221  CE  LYS A 287      15.996  47.627  79.907  1.00 17.22           C  
ANISOU 2221  CE  LYS A 287     2083   2288   2171    252    129    128       C  
ATOM   2222  NZ  LYS A 287      16.188  48.838  79.053  1.00 17.60           N  
ANISOU 2222  NZ  LYS A 287     2143   2326   2219    255    123    112       N  
ATOM   2223  N   THR A 288      16.516  42.986  82.490  1.00 12.28           N  
ANISOU 2223  N   THR A 288     1432   1684   1552    231    138    186       N  
ATOM   2224  CA  THR A 288      16.290  41.847  81.658  1.00 13.06           C  
ANISOU 2224  CA  THR A 288     1515   1773   1674    215    134    196       C  
ATOM   2225  C   THR A 288      16.313  42.245  80.168  1.00 12.26           C  
ANISOU 2225  C   THR A 288     1411   1660   1588    206    124    182       C  
ATOM   2226  O   THR A 288      15.873  43.320  79.780  1.00 12.47           O  
ANISOU 2226  O   THR A 288     1440   1688   1610    214    125    173       O  
ATOM   2227  CB  THR A 288      14.925  41.226  81.986  1.00 13.23           C  
ANISOU 2227  CB  THR A 288     1518   1806   1703    216    148    217       C  
ATOM   2228  OG1 THR A 288      14.945  40.848  83.368  1.00 14.87           O  
ANISOU 2228  OG1 THR A 288     1729   2026   1895    224    158    230       O  
ATOM   2229  CG2 THR A 288      14.663  39.991  81.181  1.00 13.64           C  
ANISOU 2229  CG2 THR A 288     1556   1849   1779    198    144    227       C  
ATOM   2230  N   LYS A 289      16.870  41.347  79.390  1.00 12.87           N  
ANISOU 2230  N   LYS A 289     1484   1724   1681    191    114    182       N  
ATOM   2231  CA ALYS A 289      16.897  41.457  77.925  0.70 13.82           C  
ANISOU 2231  CA ALYS A 289     1600   1834   1818    180    104    171       C  
ATOM   2232  CA BLYS A 289      16.905  41.453  77.930  0.30 13.67           C  
ANISOU 2232  CA BLYS A 289     1581   1815   1799    180    104    171       C  
ATOM   2233  C   LYS A 289      15.559  41.912  77.384  1.00 13.79           C  
ANISOU 2233  C   LYS A 289     1583   1836   1819    182    110    175       C  
ATOM   2234  O   LYS A 289      14.486  41.378  77.765  1.00 14.70           O  
ANISOU 2234  O   LYS A 289     1684   1961   1939    183    120    191       O  
ATOM   2235  CB ALYS A 289      17.231  40.089  77.343  0.70 15.26           C  
ANISOU 2235  CB ALYS A 289     1776   2005   2019    164     98    177       C  
ATOM   2236  CB BLYS A 289      17.272  40.082  77.354  0.30 14.43           C  
ANISOU 2236  CB BLYS A 289     1671   1899   1914    164     98    177       C  
ATOM   2237  CG ALYS A 289      17.050  39.959  75.836  0.70 16.03           C  
ANISOU 2237  CG ALYS A 289     1866   2092   2134    150     90    169       C  
ATOM   2238  CG BLYS A 289      17.129  39.912  75.847  0.30 14.92           C  
ANISOU 2238  CG BLYS A 289     1726   1950   1993    150     89    168       C  
ATOM   2239  CD ALYS A 289      17.329  38.521  75.383  0.70 16.07           C  
ANISOU 2239  CD ALYS A 289     1864   2084   2156    134     86    175       C  
ATOM   2240  CD BLYS A 289      17.237  38.431  75.496  0.30 15.19           C  
ANISOU 2240  CD BLYS A 289     1752   1973   2045    135     87    177       C  
ATOM   2241  CE ALYS A 289      17.813  38.410  73.920  0.70 16.92           C  
ANISOU 2241  CE ALYS A 289     1974   2179   2277    122     74    160       C  
ATOM   2242  CE BLYS A 289      17.201  38.143  73.998  0.30 15.56           C  
ANISOU 2242  CE BLYS A 289     1794   2009   2108    120     78    167       C  
ATOM   2243  NZ ALYS A 289      18.914  39.366  73.610  0.70 16.15           N  
ANISOU 2243  NZ ALYS A 289     1890   2078   2169    127     65    143       N  
ATOM   2244  NZ BLYS A 289      17.608  36.739  73.711  0.30 15.88           N  
ANISOU 2244  NZ BLYS A 289     1833   2036   2165    106     75    172       N  
ATOM   2245  N   VAL A 290      15.580  42.897  76.492  1.00 14.23           N  
ANISOU 2245  N   VAL A 290     1644   1889   1875    184    104    161       N  
ATOM   2246  CA  VAL A 290      14.342  43.383  75.839  1.00 14.96           C  
ANISOU 2246  CA  VAL A 290     1724   1988   1974    187    108    164       C  
ATOM   2247  C   VAL A 290      14.028  42.429  74.702  1.00 14.76           C  
ANISOU 2247  C   VAL A 290     1683   1956   1968    169    100    167       C  
ATOM   2248  O   VAL A 290      14.896  42.130  73.864  1.00 14.51           O  
ANISOU 2248  O   VAL A 290     1658   1912   1945    157     89    157       O  
ATOM   2249  CB  VAL A 290      14.516  44.814  75.304  1.00 15.69           C  
ANISOU 2249  CB  VAL A 290     1827   2078   2058    197    104    148       C  
ATOM   2250  CG1 VAL A 290      13.276  45.304  74.557  1.00 16.14           C  
ANISOU 2250  CG1 VAL A 290     1869   2141   2121    201    107    153       C  
ATOM   2251  CG2 VAL A 290      14.793  45.791  76.426  1.00 16.84           C  
ANISOU 2251  CG2 VAL A 290     1988   2227   2182    215    111    143       C  
ATOM   2252  N   ALA A 291      12.770  41.950  74.639  1.00 15.24           N  
ANISOU 2252  N   ALA A 291     1724   2027   2038    165    107    182       N  
ATOM   2253  CA  ALA A 291      12.401  40.937  73.661  1.00 15.68           C  
ANISOU 2253  CA  ALA A 291     1766   2078   2113    145    101    186       C  
ATOM   2254  C   ALA A 291      12.498  41.547  72.261  1.00 14.50           C  
ANISOU 2254  C   ALA A 291     1617   1923   1968    140     89    172       C  
ATOM   2255  O   ALA A 291      11.948  42.605  71.999  1.00 15.13           O  
ANISOU 2255  O   ALA A 291     1696   2012   2043    152     91    169       O  
ATOM   2256  CB  ALA A 291      10.990  40.457  73.902  1.00 16.70           C  
ANISOU 2256  CB  ALA A 291     1873   2221   2249    143    110    204       C  
ATOM   2257  N   TRP A 292      13.117  40.838  71.341  1.00 15.57           N  
ANISOU 2257  N   TRP A 292     1755   2047   2116    124     78    164       N  
ATOM   2258  CA  TRP A 292      13.255  41.375  69.967  1.00 14.40           C  
ANISOU 2258  CA  TRP A 292     1608   1894   1971    118     67    151       C  
ATOM   2259  C   TRP A 292      11.900  41.615  69.336  1.00 15.02           C  
ANISOU 2259  C   TRP A 292     1668   1986   2055    116     67    158       C  
ATOM   2260  O   TRP A 292      11.754  42.608  68.650  1.00 12.94           O  
ANISOU 2260  O   TRP A 292     1406   1726   1786    123     63    151       O  
ATOM   2261  CB  TRP A 292      14.007  40.404  69.096  1.00 14.75           C  
ANISOU 2261  CB  TRP A 292     1655   1924   2027     99     56    143       C  
ATOM   2262  CG  TRP A 292      15.395  40.173  69.571  1.00 14.40           C  
ANISOU 2262  CG  TRP A 292     1627   1867   1978    101     55    135       C  
ATOM   2263  CD1 TRP A 292      15.952  38.986  70.005  1.00 15.29           C  
ANISOU 2263  CD1 TRP A 292     1742   1970   2098     93     56    140       C  
ATOM   2264  CD2 TRP A 292      16.446  41.120  69.553  1.00 14.61           C  
ANISOU 2264  CD2 TRP A 292     1670   1889   1993    110     50    122       C  
ATOM   2265  NE1 TRP A 292      17.253  39.195  70.364  1.00 14.78           N  
ANISOU 2265  NE1 TRP A 292     1692   1897   2025     99     53    131       N  
ATOM   2266  CE2 TRP A 292      17.589  40.489  70.073  1.00 13.87           C  
ANISOU 2266  CE2 TRP A 292     1586   1786   1899    108     49    120       C  
ATOM   2267  CE3 TRP A 292      16.505  42.468  69.215  1.00 13.58           C  
ANISOU 2267  CE3 TRP A 292     1547   1762   1852    120     48    113       C  
ATOM   2268  CZ2 TRP A 292      18.800  41.148  70.203  1.00 13.39           C  
ANISOU 2268  CZ2 TRP A 292     1540   1719   1827    114     45    108       C  
ATOM   2269  CZ3 TRP A 292      17.710  43.135  69.373  1.00 14.67           C  
ANISOU 2269  CZ3 TRP A 292     1701   1892   1979    126     44    101       C  
ATOM   2270  CH2 TRP A 292      18.818  42.490  69.850  1.00 13.99           C  
ANISOU 2270  CH2 TRP A 292     1623   1799   1893    122     42     99       C  
ATOM   2271  N   ALA A 293      10.945  40.724  69.549  1.00 15.80           N  
ANISOU 2271  N   ALA A 293     1748   2092   2163    107     72    173       N  
ATOM   2272  CA  ALA A 293       9.600  40.960  69.054  1.00 17.31           C  
ANISOU 2272  CA  ALA A 293     1919   2300   2359    106     73    181       C  
ATOM   2273  C   ALA A 293       8.942  42.238  69.564  1.00 17.57           C  
ANISOU 2273  C   ALA A 293     1949   2347   2379    130     82    187       C  
ATOM   2274  O   ALA A 293       8.041  42.749  68.907  1.00 17.66           O  
ANISOU 2274  O   ALA A 293     1948   2371   2393    133     80    190       O  
ATOM   2275  CB  ALA A 293       8.693  39.765  69.329  1.00 18.51           C  
ANISOU 2275  CB  ALA A 293     2052   2458   2524     92     78    197       C  
ATOM   2276  N   LYS A 294       9.309  42.732  70.742  1.00 18.47           N  
ANISOU 2276  N   LYS A 294     2076   2461   2481    147     93    188       N  
ATOM   2277  CA  LYS A 294       8.781  44.003  71.230  1.00 19.20           C  
ANISOU 2277  CA  LYS A 294     2170   2565   2561    171    102    190       C  
ATOM   2278  C   LYS A 294       9.445  45.223  70.583  1.00 18.28           C  
ANISOU 2278  C   LYS A 294     2071   2440   2436    180     95    174       C  
ATOM   2279  O   LYS A 294       8.796  46.211  70.295  1.00 19.42           O  
ANISOU 2279  O   LYS A 294     2211   2591   2576    194     97    175       O  
ATOM   2280  CB  LYS A 294       8.885  44.074  72.746  1.00 23.04           C  
ANISOU 2280  CB  LYS A 294     2664   3055   3035    185    116    196       C  
ATOM   2281  CG  LYS A 294       8.070  42.973  73.430  1.00 29.13           C  
ANISOU 2281  CG  LYS A 294     3418   3838   3814    177    125    215       C  
ATOM   2282  CD  LYS A 294       7.548  43.407  74.795  1.00 34.64           C  
ANISOU 2282  CD  LYS A 294     4115   4549   4499    197    143    226       C  
ATOM   2283  CE  LYS A 294       7.442  42.211  75.732  1.00 40.70           C  
ANISOU 2283  CE  LYS A 294     4875   5319   5269    189    151    241       C  
ATOM   2284  NZ  LYS A 294       6.430  41.217  75.273  1.00 41.33           N  
ANISOU 2284  NZ  LYS A 294     4929   5407   5366    171    151    256       N  
ATOM   2285  N   LEU A 295      10.718  45.089  70.230  1.00 16.43           N  
ANISOU 2285  N   LEU A 295     1854   2189   2201    171     85    160       N  
ATOM   2286  CA  LEU A 295      11.436  46.120  69.535  1.00 16.94           C  
ANISOU 2286  CA  LEU A 295     1934   2244   2260    176     77    145       C  
ATOM   2287  C   LEU A 295      11.082  46.185  68.054  1.00 15.42           C  
ANISOU 2287  C   LEU A 295     1731   2052   2075    166     66    142       C  
ATOM   2288  O   LEU A 295      11.115  47.274  67.436  1.00 16.01           O  
ANISOU 2288  O   LEU A 295     1813   2126   2145    176     63    136       O  
ATOM   2289  CB  LEU A 295      12.916  45.862  69.708  1.00 18.41           C  
ANISOU 2289  CB  LEU A 295     2139   2414   2442    169     71    132       C  
ATOM   2290  CG  LEU A 295      13.321  46.113  71.136  1.00 21.94           C  
ANISOU 2290  CG  LEU A 295     2599   2862   2877    182     81    133       C  
ATOM   2291  CD1 LEU A 295      14.735  45.597  71.331  1.00 22.78           C  
ANISOU 2291  CD1 LEU A 295     2718   2955   2981    173     74    123       C  
ATOM   2292  CD2 LEU A 295      13.197  47.590  71.461  1.00 22.77           C  
ANISOU 2292  CD2 LEU A 295     2716   2968   2968    202     86    128       C  
ATOM   2293  N   PHE A 296      10.711  45.027  67.503  1.00 15.42           N  
ANISOU 2293  N   PHE A 296     1716   2055   2088    147     60    148       N  
ATOM   2294  CA  PHE A 296      10.500  44.877  66.058  1.00 14.93           C  
ANISOU 2294  CA  PHE A 296     1645   1993   2034    134     48    143       C  
ATOM   2295  C   PHE A 296       9.183  44.143  65.840  1.00 15.09           C  
ANISOU 2295  C   PHE A 296     1639   2029   2064    124     49    157       C  
ATOM   2296  O   PHE A 296       9.158  43.026  65.348  1.00 14.69           O  
ANISOU 2296  O   PHE A 296     1581   1976   2025    103     42    157       O  
ATOM   2297  CB  PHE A 296      11.675  44.092  65.407  1.00 14.56           C  
ANISOU 2297  CB  PHE A 296     1610   1931   1993    115     37    130       C  
ATOM   2298  CG  PHE A 296      13.006  44.770  65.504  1.00 14.48           C  
ANISOU 2298  CG  PHE A 296     1622   1907   1973    122     35    116       C  
ATOM   2299  CD1 PHE A 296      13.423  45.709  64.557  1.00 14.99           C  
ANISOU 2299  CD1 PHE A 296     1696   1968   2033    125     28    106       C  
ATOM   2300  CD2 PHE A 296      13.886  44.429  66.501  1.00 15.23           C  
ANISOU 2300  CD2 PHE A 296     1729   1993   2065    124     40    114       C  
ATOM   2301  CE1 PHE A 296      14.662  46.305  64.635  1.00 14.68           C  
ANISOU 2301  CE1 PHE A 296     1677   1916   1986    129     26     94       C  
ATOM   2302  CE2 PHE A 296      15.127  45.053  66.605  1.00 14.91           C  
ANISOU 2302  CE2 PHE A 296     1708   1941   2015    129     37    101       C  
ATOM   2303  CZ  PHE A 296      15.504  45.999  65.695  1.00 14.17           C  
ANISOU 2303  CZ  PHE A 296     1623   1844   1918    131     30     92       C  
ATOM   2304  N   PRO A 297       8.078  44.781  66.197  1.00 15.73           N  
ANISOU 2304  N   PRO A 297     1707   2127   2142    139     57    170       N  
ATOM   2305  CA  PRO A 297       6.816  44.066  66.259  1.00 17.45           C  
ANISOU 2305  CA  PRO A 297     1900   2362   2370    131     60    185       C  
ATOM   2306  C   PRO A 297       6.242  43.694  64.909  1.00 18.02           C  
ANISOU 2306  C   PRO A 297     1955   2441   2451    114     47    185       C  
ATOM   2307  O   PRO A 297       5.325  42.853  64.824  1.00 19.48           O  
ANISOU 2307  O   PRO A 297     2119   2638   2646    100     47    196       O  
ATOM   2308  CB  PRO A 297       5.908  45.048  67.014  1.00 16.97           C  
ANISOU 2308  CB  PRO A 297     1831   2317   2301    156     74    197       C  
ATOM   2309  CG  PRO A 297       6.451  46.397  66.687  1.00 16.78           C  
ANISOU 2309  CG  PRO A 297     1824   2285   2265    174     72    187       C  
ATOM   2310  CD  PRO A 297       7.945  46.176  66.661  1.00 16.29           C  
ANISOU 2310  CD  PRO A 297     1787   2201   2201    165     65    170       C  
ATOM   2311  N   LYS A 298       6.762  44.253  63.836  1.00 17.82           N  
ANISOU 2311  N   LYS A 298     1939   2409   2421    113     36    173       N  
ATOM   2312  CA  LYS A 298       6.224  43.878  62.515  1.00 19.89           C  
ANISOU 2312  CA  LYS A 298     2187   2681   2691     95     22    173       C  
ATOM   2313  C   LYS A 298       7.196  43.045  61.676  1.00 18.74           C  
ANISOU 2313  C   LYS A 298     2052   2519   2550     73     10    157       C  
ATOM   2314  O   LYS A 298       6.986  42.865  60.486  1.00 19.86           O  
ANISOU 2314  O   LYS A 298     2187   2666   2694     59     -2    152       O  
ATOM   2315  CB  LYS A 298       5.780  45.122  61.728  1.00 22.52           C  
ANISOU 2315  CB  LYS A 298     2516   3025   3016    110     18    174       C  
ATOM   2316  CG  LYS A 298       4.876  46.090  62.512  1.00 25.14           C  
ANISOU 2316  CG  LYS A 298     2839   3372   3343    136     30    189       C  
ATOM   2317  CD  LYS A 298       5.197  47.538  62.175  1.00 29.21           C  
ANISOU 2317  CD  LYS A 298     3368   3882   3847    158     30    184       C  
ATOM   2318  CE  LYS A 298       6.637  47.964  62.507  1.00 31.88           C  
ANISOU 2318  CE  LYS A 298     3738   4197   4178    163     32    168       C  
ATOM   2319  NZ  LYS A 298       6.901  48.624  63.836  1.00 30.64           N  
ANISOU 2319  NZ  LYS A 298     3595   4034   4013    184     47    169       N  
ATOM   2320  N   SER A 299       8.267  42.562  62.280  1.00 16.49           N  
ANISOU 2320  N   SER A 299     1785   2216   2265     70     14    149       N  
ATOM   2321  CA  SER A 299       9.309  41.839  61.543  1.00 14.66           C  
ANISOU 2321  CA  SER A 299     1567   1967   2037     52      4    133       C  
ATOM   2322  C   SER A 299       9.083  40.338  61.588  1.00 14.48           C  
ANISOU 2322  C   SER A 299     1535   1940   2028     30      3    135       C  
ATOM   2323  O   SER A 299       8.535  39.810  62.552  1.00 14.01           O  
ANISOU 2323  O   SER A 299     1466   1884   1974     30     12    148       O  
ATOM   2324  CB  SER A 299      10.660  42.182  62.165  1.00 14.23           C  
ANISOU 2324  CB  SER A 299     1535   1895   1975     63      9    124       C  
ATOM   2325  OG  SER A 299      10.918  43.573  62.029  1.00 13.80           O  
ANISOU 2325  OG  SER A 299     1492   1843   1910     81      9    120       O  
ATOM   2326  N   ASP A 300       9.611  39.630  60.599  1.00 14.86           N  
ANISOU 2326  N   ASP A 300     1588   1977   2080     11     -7    122       N  
ATOM   2327  CA  ASP A 300       9.482  38.213  60.504  1.00 16.10           C  
ANISOU 2327  CA  ASP A 300     1740   2127   2251    -11     -9    122       C  
ATOM   2328  C   ASP A 300      10.166  37.507  61.680  1.00 15.62           C  
ANISOU 2328  C   ASP A 300     1689   2049   2194     -9      1    125       C  
ATOM   2329  O   ASP A 300      11.295  37.867  62.045  1.00 13.70           O  
ANISOU 2329  O   ASP A 300     1465   1795   1945      3      4    117       O  
ATOM   2330  CB  ASP A 300      10.078  37.746  59.179  1.00 19.65           C  
ANISOU 2330  CB  ASP A 300     2198   2567   2702    -29    -22    104       C  
ATOM   2331  CG  ASP A 300       9.973  36.260  58.995  1.00 23.67           C  
ANISOU 2331  CG  ASP A 300     2703   3064   3225    -53    -24    101       C  
ATOM   2332  OD1 ASP A 300       8.929  35.794  58.492  1.00 23.20           O  
ANISOU 2332  OD1 ASP A 300     2627   3017   3172    -69    -30    105       O  
ATOM   2333  OD2 ASP A 300      10.904  35.542  59.396  1.00 24.22           O  
ANISOU 2333  OD2 ASP A 300     2788   3115   3300    -55    -20     95       O  
ATOM   2334  N   SER A 301       9.503  36.548  62.297  1.00 15.25           N  
ANISOU 2334  N   SER A 301     1632   2004   2159    -20      7    137       N  
ATOM   2335  CA  SER A 301      10.051  35.795  63.443  1.00 15.53           C  
ANISOU 2335  CA  SER A 301     1676   2026   2200    -18     17    143       C  
ATOM   2336  C   SER A 301      11.389  35.121  63.167  1.00 14.27           C  
ANISOU 2336  C   SER A 301     1536   1843   2043    -24     14    128       C  
ATOM   2337  O   SER A 301      12.214  35.056  64.053  1.00 14.68           O  
ANISOU 2337  O   SER A 301     1600   1885   2093    -13     20    130       O  
ATOM   2338  CB  SER A 301       9.042  34.748  63.968  1.00 17.49           C  
ANISOU 2338  CB  SER A 301     1907   2277   2460    -33     23    158       C  
ATOM   2339  OG  SER A 301       8.827  33.775  62.972  1.00 21.14           O  
ANISOU 2339  OG  SER A 301     2365   2732   2934    -58     14    150       O  
ATOM   2340  N   LYS A 302      11.562  34.589  61.959  1.00 13.77           N  
ANISOU 2340  N   LYS A 302     1474   1771   1985    -42      3    115       N  
ATOM   2341  CA  LYS A 302      12.842  33.985  61.603  1.00 13.81           C  
ANISOU 2341  CA  LYS A 302     1498   1755   1994    -46      0    100       C  
ATOM   2342  C   LYS A 302      13.960  35.002  61.488  1.00 12.94           C  
ANISOU 2342  C   LYS A 302     1403   1643   1870    -29     -1     90       C  
ATOM   2343  O   LYS A 302      15.081  34.745  61.949  1.00 12.08           O  
ANISOU 2343  O   LYS A 302     1308   1519   1761    -22      2     85       O  
ATOM   2344  CB  LYS A 302      12.763  33.142  60.328  1.00 14.92           C  
ANISOU 2344  CB  LYS A 302     1638   1887   2143    -69    -10     87       C  
ATOM   2345  CG  LYS A 302      11.810  31.939  60.467  1.00 16.86           C  
ANISOU 2345  CG  LYS A 302     1872   2130   2404    -90     -8     95       C  
ATOM   2346  CD  LYS A 302      11.727  31.197  59.165  1.00 18.51           C  
ANISOU 2346  CD  LYS A 302     2082   2331   2619   -113    -19     80       C  
ATOM   2347  CE  LYS A 302      10.892  31.939  58.171  1.00 20.67           C  
ANISOU 2347  CE  LYS A 302     2342   2626   2885   -118    -29     76       C  
ATOM   2348  NZ  LYS A 302      10.088  30.902  57.469  1.00 23.50           N  
ANISOU 2348  NZ  LYS A 302     2691   2984   3255   -146    -36     73       N  
ATOM   2349  N   ALA A 303      13.661  36.177  60.950  1.00 12.32           N  
ANISOU 2349  N   ALA A 303     1321   1579   1781    -21     -6     87       N  
ATOM   2350  CA  ALA A 303      14.665  37.264  60.931  1.00 11.78           C  
ANISOU 2350  CA  ALA A 303     1267   1509   1700     -4     -7     79       C  
ATOM   2351  C   ALA A 303      15.079  37.591  62.361  1.00 11.23           C  
ANISOU 2351  C   ALA A 303     1203   1438   1625     13      3     88       C  
ATOM   2352  O   ALA A 303      16.229  37.844  62.622  1.00 10.71           O  
ANISOU 2352  O   ALA A 303     1152   1363   1554     21      4     81       O  
ATOM   2353  CB  ALA A 303      14.122  38.473  60.244  1.00 11.36           C  
ANISOU 2353  CB  ALA A 303     1208   1471   1636      3    -12     78       C  
ATOM   2354  N   LEU A 304      14.129  37.662  63.291  1.00 11.23           N  
ANISOU 2354  N   LEU A 304     1192   1448   1626     19     11    103       N  
ATOM   2355  CA  LEU A 304      14.456  38.016  64.675  1.00 10.98           C  
ANISOU 2355  CA  LEU A 304     1167   1417   1587     36     21    112       C  
ATOM   2356  C   LEU A 304      15.227  36.967  65.399  1.00 11.12           C  
ANISOU 2356  C   LEU A 304     1192   1421   1611     32     26    114       C  
ATOM   2357  O   LEU A 304      16.070  37.285  66.222  1.00 11.20           O  
ANISOU 2357  O   LEU A 304     1214   1428   1614     45     30    114       O  
ATOM   2358  CB  LEU A 304      13.178  38.357  65.412  1.00 11.24           C  
ANISOU 2358  CB  LEU A 304     1186   1468   1619     43     29    128       C  
ATOM   2359  CG  LEU A 304      12.459  39.606  64.884  1.00 11.73           C  
ANISOU 2359  CG  LEU A 304     1240   1544   1672     53     27    128       C  
ATOM   2360  CD1 LEU A 304      11.268  39.976  65.770  1.00 12.75           C  
ANISOU 2360  CD1 LEU A 304     1355   1690   1798     64     37    145       C  
ATOM   2361  CD2 LEU A 304      13.342  40.821  64.692  1.00 11.91           C  
ANISOU 2361  CD2 LEU A 304     1279   1563   1682     67     24    116       C  
ATOM   2362  N   ASP A 305      14.990  35.702  65.045  1.00 10.83           N  
ANISOU 2362  N   ASP A 305     1150   1375   1589     15     24    115       N  
ATOM   2363  CA  ASP A 305      15.748  34.615  65.616  1.00 11.44           C  
ANISOU 2363  CA  ASP A 305     1236   1436   1674     11     28    118       C  
ATOM   2364  C   ASP A 305      17.191  34.740  65.176  1.00 11.24           C  
ANISOU 2364  C   ASP A 305     1227   1399   1645     15     23    102       C  
ATOM   2365  O   ASP A 305      18.092  34.582  65.992  1.00 11.72           O  
ANISOU 2365  O   ASP A 305     1297   1453   1703     25     27    105       O  
ATOM   2366  CB  ASP A 305      15.179  33.245  65.279  1.00 12.50           C  
ANISOU 2366  CB  ASP A 305     1363   1561   1825     -9     28    122       C  
ATOM   2367  CG  ASP A 305      15.962  32.154  65.959  1.00 14.31           C  
ANISOU 2367  CG  ASP A 305     1601   1772   2062    -10     34    126       C  
ATOM   2368  OD1 ASP A 305      15.793  31.994  67.215  1.00 17.69           O  
ANISOU 2368  OD1 ASP A 305     2028   2203   2489     -1     43    143       O  
ATOM   2369  OD2 ASP A 305      16.862  31.549  65.332  1.00 14.65           O  
ANISOU 2369  OD2 ASP A 305     1656   1799   2112    -16     29    114       O  
ATOM   2370  N   LEU A 306      17.409  35.027  63.890  1.00 10.59           N  
ANISOU 2370  N   LEU A 306     1147   1315   1562      8     14     87       N  
ATOM   2371  CA  LEU A 306      18.755  35.150  63.392  1.00 10.38           C  
ANISOU 2371  CA  LEU A 306     1133   1277   1531     11      9     73       C  
ATOM   2372  C   LEU A 306      19.413  36.403  64.006  1.00  9.53           C  
ANISOU 2372  C   LEU A 306     1033   1178   1408     29     11     72       C  
ATOM   2373  O   LEU A 306      20.572  36.373  64.417  1.00  9.02           O  
ANISOU 2373  O   LEU A 306      980   1107   1342     36     11     69       O  
ATOM   2374  CB  LEU A 306      18.773  35.173  61.855  1.00 10.46           C  
ANISOU 2374  CB  LEU A 306     1144   1286   1543     -1      0     58       C  
ATOM   2375  CG  LEU A 306      20.139  35.271  61.193  1.00 10.88           C  
ANISOU 2375  CG  LEU A 306     1210   1330   1593      1     -4     42       C  
ATOM   2376  CD1 LEU A 306      21.081  34.273  61.726  1.00 10.89           C  
ANISOU 2376  CD1 LEU A 306     1220   1316   1603      2      0     43       C  
ATOM   2377  CD2 LEU A 306      19.969  35.115  59.694  1.00 11.11           C  
ANISOU 2377  CD2 LEU A 306     1239   1358   1624    -13    -12     29       C  
ATOM   2378  N   LEU A 307      18.682  37.509  64.108  1.00  9.80           N  
ANISOU 2378  N   LEU A 307     1063   1227   1434     37     11     76       N  
ATOM   2379  CA  LEU A 307      19.158  38.726  64.752  1.00  9.85           C  
ANISOU 2379  CA  LEU A 307     1078   1239   1426     53     13     75       C  
ATOM   2380  C   LEU A 307      19.642  38.395  66.161  1.00 11.03           C  
ANISOU 2380  C   LEU A 307     1232   1387   1573     62     20     84       C  
ATOM   2381  O   LEU A 307      20.740  38.858  66.570  1.00 10.68           O  
ANISOU 2381  O   LEU A 307     1198   1339   1519     71     19     78       O  
ATOM   2382  CB  LEU A 307      18.058  39.795  64.826  1.00 10.21           C  
ANISOU 2382  CB  LEU A 307     1115   1299   1463     61     15     81       C  
ATOM   2383  CG  LEU A 307      18.446  41.094  65.484  1.00 10.38           C  
ANISOU 2383  CG  LEU A 307     1147   1326   1471     78     18     80       C  
ATOM   2384  CD1 LEU A 307      19.506  41.801  64.639  1.00 10.56           C  
ANISOU 2384  CD1 LEU A 307     1182   1343   1489     78     10     65       C  
ATOM   2385  CD2 LEU A 307      17.221  41.967  65.603  1.00 11.48           C  
ANISOU 2385  CD2 LEU A 307     1278   1479   1605     87     22     87       C  
ATOM   2386  N   ASP A 308      18.821  37.619  66.905  1.00 10.93           N  
ANISOU 2386  N   ASP A 308     1210   1375   1566     60     27     99       N  
ATOM   2387  CA  ASP A 308      19.160  37.230  68.275  1.00 11.69           C  
ANISOU 2387  CA  ASP A 308     1310   1472   1660     69     35    110       C  
ATOM   2388  C   ASP A 308      20.514  36.506  68.385  1.00 11.53           C  
ANISOU 2388  C   ASP A 308     1299   1438   1643     68     32    105       C  
ATOM   2389  O   ASP A 308      21.318  36.791  69.261  1.00 13.08           O  
ANISOU 2389  O   ASP A 308     1503   1636   1829     79     34    106       O  
ATOM   2390  CB  ASP A 308      18.006  36.406  68.840  1.00 12.96           C  
ANISOU 2390  CB  ASP A 308     1458   1636   1829     64     43    126       C  
ATOM   2391  CG  ASP A 308      18.226  36.000  70.280  1.00 15.13           C  
ANISOU 2391  CG  ASP A 308     1736   1913   2100     73     51    140       C  
ATOM   2392  OD1 ASP A 308      18.479  36.860  71.114  1.00 14.99           O  
ANISOU 2392  OD1 ASP A 308     1724   1904   2067     87     55    141       O  
ATOM   2393  OD2 ASP A 308      18.256  34.783  70.528  1.00 21.02           O  
ANISOU 2393  OD2 ASP A 308     2480   2650   2858     65     55    149       O  
ATOM   2394  N   ARG A 309      20.768  35.674  67.412  1.00 11.27           N  
ANISOU 2394  N   ARG A 309     1266   1393   1622     55     28     98       N  
ATOM   2395  CA  ARG A 309      21.972  34.833  67.349  1.00 11.24           C  
ANISOU 2395  CA  ARG A 309     1271   1376   1626     54     26     93       C  
ATOM   2396  C   ARG A 309      23.204  35.619  66.954  1.00 10.62           C  
ANISOU 2396  C   ARG A 309     1201   1297   1537     60     20     79       C  
ATOM   2397  O   ARG A 309      24.313  35.287  67.326  1.00 11.07           O  
ANISOU 2397  O   ARG A 309     1265   1348   1594     65     20     78       O  
ATOM   2398  CB  ARG A 309      21.725  33.715  66.398  1.00 11.76           C  
ANISOU 2398  CB  ARG A 309     1333   1427   1707     39     25     89       C  
ATOM   2399  CG  ARG A 309      20.705  32.728  66.938  1.00 13.28           C  
ANISOU 2399  CG  ARG A 309     1518   1617   1911     31     31    104       C  
ATOM   2400  CD  ARG A 309      20.349  31.670  65.903  1.00 15.10           C  
ANISOU 2400  CD  ARG A 309     1746   1834   2158     13     29     98       C  
ATOM   2401  NE  ARG A 309      19.309  30.740  66.408  1.00 18.29           N  
ANISOU 2401  NE  ARG A 309     2141   2234   2573      3     35    114       N  
ATOM   2402  CZ  ARG A 309      19.594  29.631  67.114  1.00 20.71           C  
ANISOU 2402  CZ  ARG A 309     2452   2527   2890      3     42    125       C  
ATOM   2403  NH1 ARG A 309      20.858  29.328  67.415  1.00 20.96           N  
ANISOU 2403  NH1 ARG A 309     2494   2548   2921     13     42    123       N  
ATOM   2404  NH2 ARG A 309      18.604  28.809  67.514  1.00 24.60           N  
ANISOU 2404  NH2 ARG A 309     2936   3016   3393     -8     48    139       N  
ATOM   2405  N   MET A 310      22.970  36.715  66.244  1.00  9.82           N  
ANISOU 2405  N   MET A 310     1100   1203   1427     60     15     70       N  
ATOM   2406  CA  MET A 310      24.088  37.601  65.797  1.00  9.81           C  
ANISOU 2406  CA  MET A 310     1108   1203   1418     64     10     57       C  
ATOM   2407  C   MET A 310      24.465  38.632  66.865  1.00 10.02           C  
ANISOU 2407  C   MET A 310     1139   1238   1428     78     11     60       C  
ATOM   2408  O   MET A 310      25.630  39.032  66.986  1.00 10.72           O  
ANISOU 2408  O   MET A 310     1236   1327   1511     82      8     53       O  
ATOM   2409  CB  MET A 310      23.783  38.350  64.507  1.00 10.21           C  
ANISOU 2409  CB  MET A 310     1158   1256   1466     58      4     45       C  
ATOM   2410  CG  MET A 310      23.581  37.390  63.343  1.00 11.04           C  
ANISOU 2410  CG  MET A 310     1260   1353   1584     44      1     39       C  
ATOM   2411  SD  MET A 310      23.137  38.415  61.894  1.00 15.41           S  
ANISOU 2411  SD  MET A 310     1811   1913   2130     39     -6     28       S  
ATOM   2412  CE  MET A 310      23.507  37.294  60.656  1.00 15.78           C  
ANISOU 2412  CE  MET A 310     1859   1948   2188     25    -10     16       C  
ATOM   2413  N   LEU A 311      23.492  39.045  67.628  1.00  9.95           N  
ANISOU 2413  N   LEU A 311     1127   1238   1414     83     16     69       N  
ATOM   2414  CA  LEU A 311      23.649  40.105  68.645  1.00 10.08           C  
ANISOU 2414  CA  LEU A 311     1150   1264   1415     96     19     71       C  
ATOM   2415  C   LEU A 311      23.717  39.517  70.031  1.00 12.03           C  
ANISOU 2415  C   LEU A 311     1397   1514   1659    103     25     84       C  
ATOM   2416  O   LEU A 311      23.052  39.993  70.953  1.00 14.18           O  
ANISOU 2416  O   LEU A 311     1669   1796   1922    112     31     91       O  
ATOM   2417  CB  LEU A 311      22.595  41.210  68.553  1.00 10.00           C  
ANISOU 2417  CB  LEU A 311     1138   1263   1398    101     21     71       C  
ATOM   2418  CG  LEU A 311      22.539  42.004  67.245  1.00  9.98           C  
ANISOU 2418  CG  LEU A 311     1137   1259   1396     96     15     60       C  
ATOM   2419  CD1 LEU A 311      21.505  43.087  67.278  1.00  9.92           C  
ANISOU 2419  CD1 LEU A 311     1128   1261   1381    104     18     62       C  
ATOM   2420  CD2 LEU A 311      23.913  42.631  66.937  1.00  9.47           C  
ANISOU 2420  CD2 LEU A 311     1084   1191   1325     96      8     47       C  
ATOM   2421  N   THR A 312      24.512  38.485  70.193  1.00 11.94           N  
ANISOU 2421  N   THR A 312     1386   1495   1654    100     24     86       N  
ATOM   2422  CA  THR A 312      24.826  37.947  71.551  1.00 11.97           C  
ANISOU 2422  CA  THR A 312     1392   1503   1655    108     29     99       C  
ATOM   2423  C   THR A 312      25.866  38.803  72.245  1.00 11.50           C  
ANISOU 2423  C   THR A 312     1341   1450   1578    117     25     94       C  
ATOM   2424  O   THR A 312      26.831  39.242  71.635  1.00 11.05           O  
ANISOU 2424  O   THR A 312     1289   1391   1519    115     18     81       O  
ATOM   2425  CB  THR A 312      25.296  36.485  71.511  1.00 13.91           C  
ANISOU 2425  CB  THR A 312     1634   1736   1913    104     30    106       C  
ATOM   2426  OG1 THR A 312      26.603  36.402  70.844  1.00 14.79           O  
ANISOU 2426  OG1 THR A 312     1751   1841   2028    102     22     94       O  
ATOM   2427  CG2 THR A 312      24.214  35.693  70.796  1.00 13.98           C  
ANISOU 2427  CG2 THR A 312     1635   1738   1939     93     33    110       C  
ATOM   2428  N   PHE A 313      25.697  39.034  73.540  1.00 10.95           N  
ANISOU 2428  N   PHE A 313     1274   1391   1496    127     30    103       N  
ATOM   2429  CA  PHE A 313      26.679  39.788  74.289  1.00 11.51           C  
ANISOU 2429  CA  PHE A 313     1354   1470   1550    134     25     97       C  
ATOM   2430  C   PHE A 313      28.044  39.098  74.293  1.00 11.68           C  
ANISOU 2430  C   PHE A 313     1375   1487   1575    133     19     97       C  
ATOM   2431  O   PHE A 313      29.050  39.732  74.048  1.00 12.96           O  
ANISOU 2431  O   PHE A 313     1542   1650   1730    132     12     85       O  
ATOM   2432  CB  PHE A 313      26.210  39.989  75.745  1.00 12.00           C  
ANISOU 2432  CB  PHE A 313     1418   1544   1597    144     32    108       C  
ATOM   2433  CG  PHE A 313      27.223  40.665  76.600  1.00 11.32           C  
ANISOU 2433  CG  PHE A 313     1341   1467   1493    150     27    103       C  
ATOM   2434  CD1 PHE A 313      27.337  42.047  76.632  1.00 11.98           C  
ANISOU 2434  CD1 PHE A 313     1434   1555   1562    153     24     89       C  
ATOM   2435  CD2 PHE A 313      28.069  39.916  77.402  1.00 11.35           C  
ANISOU 2435  CD2 PHE A 313     1344   1475   1493    154     25    112       C  
ATOM   2436  CE1 PHE A 313      28.289  42.653  77.457  1.00 11.79           C  
ANISOU 2436  CE1 PHE A 313     1419   1540   1521    156     19     83       C  
ATOM   2437  CE2 PHE A 313      29.016  40.485  78.192  1.00 11.84           C  
ANISOU 2437  CE2 PHE A 313     1414   1547   1537    158     19    107       C  
ATOM   2438  CZ  PHE A 313      29.142  41.851  78.241  1.00 12.06           C  
ANISOU 2438  CZ  PHE A 313     1451   1580   1551    159     15     93       C  
ATOM   2439  N   ASN A 314      28.037  37.795  74.524  1.00 11.05           N  
ANISOU 2439  N   ASN A 314     1291   1402   1507    132     23    110       N  
ATOM   2440  CA  ASN A 314      29.295  37.042  74.591  1.00 10.95           C  
ANISOU 2440  CA  ASN A 314     1277   1384   1497    134     18    112       C  
ATOM   2441  C   ASN A 314      29.725  36.645  73.181  1.00 10.39           C  
ANISOU 2441  C   ASN A 314     1205   1301   1443    125     14    101       C  
ATOM   2442  O   ASN A 314      29.010  35.929  72.505  1.00 10.31           O  
ANISOU 2442  O   ASN A 314     1190   1280   1448    119     18    103       O  
ATOM   2443  CB  ASN A 314      29.057  35.803  75.462  1.00 11.78           C  
ANISOU 2443  CB  ASN A 314     1378   1488   1608    139     25    132       C  
ATOM   2444  CG  ASN A 314      30.300  35.012  75.746  1.00 13.51           C  
ANISOU 2444  CG  ASN A 314     1597   1704   1830    144     21    137       C  
ATOM   2445  OD1 ASN A 314      31.222  34.957  74.948  1.00 12.46           O  
ANISOU 2445  OD1 ASN A 314     1465   1566   1704    141     15    127       O  
ATOM   2446  ND2 ASN A 314      30.317  34.350  76.895  1.00 14.24           N  
ANISOU 2446  ND2 ASN A 314     1690   1803   1919    152     25    155       N  
ATOM   2447  N   PRO A 315      30.908  37.112  72.752  1.00  9.52           N  
ANISOU 2447  N   PRO A 315     1096   1192   1328    125      7     89       N  
ATOM   2448  CA  PRO A 315      31.331  36.773  71.373  1.00  9.92           C  
ANISOU 2448  CA  PRO A 315     1145   1231   1393    117      4     78       C  
ATOM   2449  C   PRO A 315      31.518  35.297  71.151  1.00 10.45           C  
ANISOU 2449  C   PRO A 315     1208   1285   1476    117      8     86       C  
ATOM   2450  O   PRO A 315      31.444  34.872  70.002  1.00 10.55           O  
ANISOU 2450  O   PRO A 315     1220   1286   1501    110      8     78       O  
ATOM   2451  CB  PRO A 315      32.661  37.529  71.205  1.00  9.97           C  
ANISOU 2451  CB  PRO A 315     1154   1244   1390    118     -4     67       C  
ATOM   2452  CG  PRO A 315      33.140  37.762  72.629  1.00 10.37           C  
ANISOU 2452  CG  PRO A 315     1206   1308   1426    127     -6     76       C  
ATOM   2453  CD  PRO A 315      31.904  37.927  73.467  1.00  9.90           C  
ANISOU 2453  CD  PRO A 315     1149   1253   1360    130      0     85       C  
ATOM   2454  N   ASN A 316      31.812  34.534  72.202  1.00 10.84           N  
ANISOU 2454  N   ASN A 316     1257   1336   1526    125     11    101       N  
ATOM   2455  CA  ASN A 316      32.027  33.080  72.004  1.00 12.89           C  
ANISOU 2455  CA  ASN A 316     1515   1581   1803    126     15    110       C  
ATOM   2456  C   ASN A 316      30.726  32.375  71.639  1.00 13.80           C  
ANISOU 2456  C   ASN A 316     1629   1684   1932    118     22    115       C  
ATOM   2457  O   ASN A 316      30.745  31.260  71.101  1.00 16.90           O  
ANISOU 2457  O   ASN A 316     2021   2060   2342    115     25    117       O  
ATOM   2458  CB  ASN A 316      32.598  32.444  73.258  1.00 13.32           C  
ANISOU 2458  CB  ASN A 316     1568   1640   1854    138     16    127       C  
ATOM   2459  CG  ASN A 316      33.887  33.106  73.734  1.00 14.80           C  
ANISOU 2459  CG  ASN A 316     1755   1843   2027    146      9    124       C  
ATOM   2460  OD1 ASN A 316      34.022  33.527  74.920  1.00 19.61           O  
ANISOU 2460  OD1 ASN A 316     2364   2466   2619    153      7    133       O  
ATOM   2461  ND2 ASN A 316      34.789  33.190  72.892  1.00 13.09           N  
ANISOU 2461  ND2 ASN A 316     1537   1623   1814    144      4    113       N  
ATOM   2462  N   LYS A 317      29.605  32.947  72.037  1.00 12.63           N  
ANISOU 2462  N   LYS A 317     1479   1543   1777    116     25    118       N  
ATOM   2463  CA  LYS A 317      28.281  32.385  71.796  1.00 12.38           C  
ANISOU 2463  CA  LYS A 317     1444   1503   1756    107     31    125       C  
ATOM   2464  C   LYS A 317      27.619  32.882  70.533  1.00 12.25           C  
ANISOU 2464  C   LYS A 317     1426   1484   1744     95     28    110       C  
ATOM   2465  O   LYS A 317      26.540  32.393  70.124  1.00 12.76           O  
ANISOU 2465  O   LYS A 317     1487   1542   1820     86     32    112       O  
ATOM   2466  CB  LYS A 317      27.409  32.731  73.009  1.00 13.01           C  
ANISOU 2466  CB  LYS A 317     1522   1596   1825    112     36    139       C  
ATOM   2467  CG  LYS A 317      27.928  32.062  74.291  1.00 15.03           C  
ANISOU 2467  CG  LYS A 317     1778   1854   2076    123     40    157       C  
ATOM   2468  CD  LYS A 317      27.149  32.494  75.515  1.00 15.60           C  
ANISOU 2468  CD  LYS A 317     1851   1943   2135    129     45    170       C  
ATOM   2469  CE  LYS A 317      27.697  31.789  76.742  1.00 17.11           C  
ANISOU 2469  CE  LYS A 317     2043   2137   2322    139     48    188       C  
ATOM   2470  NZ  LYS A 317      26.923  32.249  77.917  1.00 18.10           N  
ANISOU 2470  NZ  LYS A 317     2167   2279   2431    145     54    200       N  
ATOM   2471  N   ARG A 318      28.314  33.743  69.832  1.00 10.79           N  
ANISOU 2471  N   ARG A 318     1244   1303   1552     95     21     94       N  
ATOM   2472  CA  ARG A 318      27.731  34.408  68.655  1.00 10.43           C  
ANISOU 2472  CA  ARG A 318     1198   1258   1508     86     18     80       C  
ATOM   2473  C   ARG A 318      27.801  33.495  67.450  1.00 10.16           C  
ANISOU 2473  C   ARG A 318     1163   1209   1489     76     17     72       C  
ATOM   2474  O   ARG A 318      28.800  32.763  67.276  1.00 11.44           O  
ANISOU 2474  O   ARG A 318     1327   1360   1657     78     17     70       O  
ATOM   2475  CB  ARG A 318      28.487  35.724  68.428  1.00 10.58           C  
ANISOU 2475  CB  ARG A 318     1221   1287   1512     89     12     68       C  
ATOM   2476  CG  ARG A 318      27.795  36.796  67.674  1.00 10.42           C  
ANISOU 2476  CG  ARG A 318     1200   1271   1486     84      9     59       C  
ATOM   2477  CD  ARG A 318      28.510  38.142  67.695  1.00  9.98           C  
ANISOU 2477  CD  ARG A 318     1151   1226   1416     89      4     49       C  
ATOM   2478  NE  ARG A 318      28.534  38.719  69.021  1.00  9.70           N  
ANISOU 2478  NE  ARG A 318     1118   1201   1368     98      5     57       N  
ATOM   2479  CZ  ARG A 318      29.518  39.467  69.549  1.00  9.20           C  
ANISOU 2479  CZ  ARG A 318     1060   1144   1292    103      1     52       C  
ATOM   2480  NH1 ARG A 318      30.580  39.749  68.806  1.00  9.55           N  
ANISOU 2480  NH1 ARG A 318     1106   1186   1336     99     -5     41       N  
ATOM   2481  NH2 ARG A 318      29.461  39.879  70.820  1.00  8.72           N  
ANISOU 2481  NH2 ARG A 318     1003   1093   1219    111      3     59       N  
ATOM   2482  N   ILE A 319      26.789  33.542  66.589  1.00  9.75           N  
ANISOU 2482  N   ILE A 319     1108   1154   1442     65     17     67       N  
ATOM   2483  CA  ILE A 319      26.714  32.674  65.428  1.00  9.68           C  
ANISOU 2483  CA  ILE A 319     1100   1132   1448     53     16     58       C  
ATOM   2484  C   ILE A 319      27.875  32.925  64.476  1.00  9.69           C  
ANISOU 2484  C   ILE A 319     1106   1130   1447     54     11     42       C  
ATOM   2485  O   ILE A 319      28.326  34.077  64.329  1.00  9.75           O  
ANISOU 2485  O   ILE A 319     1115   1149   1442     58      7     35       O  
ATOM   2486  CB  ILE A 319      25.327  32.803  64.756  1.00  9.89           C  
ANISOU 2486  CB  ILE A 319     1120   1160   1477     41     15     56       C  
ATOM   2487  CG1 ILE A 319      25.016  31.692  63.764  1.00 10.02           C  
ANISOU 2487  CG1 ILE A 319     1137   1162   1509     27     15     49       C  
ATOM   2488  CG2 ILE A 319      25.199  34.172  64.123  1.00  9.97           C  
ANISOU 2488  CG2 ILE A 319     1130   1184   1475     41      9     46       C  
ATOM   2489  CD1 ILE A 319      23.567  31.675  63.383  1.00 10.44           C  
ANISOU 2489  CD1 ILE A 319     1181   1219   1566     14     14     52       C  
ATOM   2490  N   THR A 320      28.338  31.899  63.796  1.00  9.34           N  
ANISOU 2490  N   THR A 320     1065   1071   1414     50     13     36       N  
ATOM   2491  CA  THR A 320      29.360  32.045  62.752  1.00  9.98           C  
ANISOU 2491  CA  THR A 320     1150   1149   1494     50     10     20       C  
ATOM   2492  C   THR A 320      28.714  32.342  61.398  1.00  9.55           C  
ANISOU 2492  C   THR A 320     1095   1096   1439     37      5      6       C  
ATOM   2493  O   THR A 320      27.546  32.159  61.230  1.00  9.33           O  
ANISOU 2493  O   THR A 320     1064   1067   1415     27      5      9       O  
ATOM   2494  CB  THR A 320      30.195  30.755  62.569  1.00 10.75           C  
ANISOU 2494  CB  THR A 320     1251   1230   1604     52     14     18       C  
ATOM   2495  OG1 THR A 320      29.341  29.742  62.011  1.00 11.30           O  
ANISOU 2495  OG1 THR A 320     1322   1284   1687     40     17     16       O  
ATOM   2496  CG2 THR A 320      30.853  30.312  63.887  1.00 11.44           C  
ANISOU 2496  CG2 THR A 320     1338   1316   1693     66     18     34       C  
ATOM   2497  N   VAL A 321      29.498  32.795  60.422  1.00  9.63           N  
ANISOU 2497  N   VAL A 321     1108   1108   1443     36      2     -8       N  
ATOM   2498  CA  VAL A 321      28.958  33.075  59.124  1.00 10.21           C  
ANISOU 2498  CA  VAL A 321     1181   1183   1514     24     -2    -20       C  
ATOM   2499  C   VAL A 321      28.317  31.867  58.430  1.00 10.49           C  
ANISOU 2499  C   VAL A 321     1219   1205   1563     12      0    -26       C  
ATOM   2500  O   VAL A 321      27.245  32.009  57.834  1.00 10.77           O  
ANISOU 2500  O   VAL A 321     1250   1243   1597      1     -4    -29       O  
ATOM   2501  CB  VAL A 321      30.001  33.807  58.214  1.00 10.24           C  
ANISOU 2501  CB  VAL A 321     1188   1192   1508     26     -5    -34       C  
ATOM   2502  CG1 VAL A 321      31.195  32.885  57.841  1.00 10.25           C  
ANISOU 2502  CG1 VAL A 321     1195   1183   1518     31     -1    -41       C  
ATOM   2503  CG2 VAL A 321      29.326  34.388  57.016  1.00 10.42           C  
ANISOU 2503  CG2 VAL A 321     1211   1222   1526     16    -10    -44       C  
ATOM   2504  N   GLU A 322      28.933  30.697  58.537  1.00 11.03           N  
ANISOU 2504  N   GLU A 322     1291   1256   1643     15      5    -27       N  
ATOM   2505  CA  GLU A 322      28.379  29.511  57.900  1.00 11.55           C  
ANISOU 2505  CA  GLU A 322     1361   1306   1722      3      7    -33       C  
ATOM   2506  C   GLU A 322      27.065  29.134  58.547  1.00 11.76           C  
ANISOU 2506  C   GLU A 322     1382   1330   1755     -6      8    -20       C  
ATOM   2507  O   GLU A 322      26.135  28.633  57.873  1.00 11.56           O  
ANISOU 2507  O   GLU A 322     1356   1300   1736    -22      6    -26       O  
ATOM   2508  CB  GLU A 322      29.344  28.347  57.985  1.00 12.64           C  
ANISOU 2508  CB  GLU A 322     1507   1425   1872     10     14    -35       C  
ATOM   2509  CG  GLU A 322      30.583  28.536  57.137  1.00 15.36           C  
ANISOU 2509  CG  GLU A 322     1855   1770   2210     16     15    -50       C  
ATOM   2510  CD  GLU A 322      31.678  29.325  57.801  1.00 16.95           C  
ANISOU 2510  CD  GLU A 322     2054   1984   2403     32     15    -43       C  
ATOM   2511  OE1 GLU A 322      31.614  29.656  59.093  1.00 15.47           O  
ANISOU 2511  OE1 GLU A 322     1862   1804   2214     40     15    -27       O  
ATOM   2512  OE2 GLU A 322      32.621  29.601  56.963  1.00 20.88           O  
ANISOU 2512  OE2 GLU A 322     2554   2486   2896     35     15    -56       O  
ATOM   2513  N   GLU A 323      27.014  29.248  59.858  1.00 11.21           N  
ANISOU 2513  N   GLU A 323     1308   1264   1685      4     11     -3       N  
ATOM   2514  CA  GLU A 323      25.759  28.922  60.579  1.00 11.99           C  
ANISOU 2514  CA  GLU A 323     1401   1363   1790     -3     13     11       C  
ATOM   2515  C   GLU A 323      24.655  29.892  60.180  1.00 11.54           C  
ANISOU 2515  C   GLU A 323     1335   1324   1724    -12      7     10       C  
ATOM   2516  O   GLU A 323      23.497  29.478  59.986  1.00 11.69           O  
ANISOU 2516  O   GLU A 323     1349   1342   1751    -25      6     13       O  
ATOM   2517  CB  GLU A 323      25.991  28.939  62.092  1.00 13.55           C  
ANISOU 2517  CB  GLU A 323     1597   1564   1987     10     18     30       C  
ATOM   2518  CG  GLU A 323      26.791  27.739  62.641  1.00 15.95           C  
ANISOU 2518  CG  GLU A 323     1907   1849   2303     17     25     37       C  
ATOM   2519  CD  GLU A 323      27.515  28.017  64.001  1.00 19.06           C  
ANISOU 2519  CD  GLU A 323     2300   2250   2690     35     28     52       C  
ATOM   2520  OE1 GLU A 323      27.381  29.114  64.697  1.00 16.03           O  
ANISOU 2520  OE1 GLU A 323     1912   1887   2293     42     26     59       O  
ATOM   2521  OE2 GLU A 323      28.283  27.057  64.408  1.00 24.28           O  
ANISOU 2521  OE2 GLU A 323     2966   2897   3361     43     34     58       O  
ATOM   2522  N   ALA A 324      25.016  31.156  60.021  1.00 10.31           N  
ANISOU 2522  N   ALA A 324     1180   1184   1555     -4      3      6       N  
ATOM   2523  CA  ALA A 324      24.054  32.184  59.708  1.00  9.74           C  
ANISOU 2523  CA  ALA A 324     1100   1128   1472     -8     -3      6       C  
ATOM   2524  C   ALA A 324      23.505  31.913  58.307  1.00  9.75           C  
ANISOU 2524  C   ALA A 324     1100   1127   1476    -24     -8     -7       C  
ATOM   2525  O   ALA A 324      22.284  31.967  58.067  1.00  9.20           O  
ANISOU 2525  O   ALA A 324     1022   1066   1408    -35    -12     -4       O  
ATOM   2526  CB  ALA A 324      24.678  33.547  59.860  1.00  9.83           C  
ANISOU 2526  CB  ALA A 324     1113   1153   1469      4     -5      5       C  
ATOM   2527  N   LEU A 325      24.381  31.558  57.364  1.00  9.42           N  
ANISOU 2527  N   LEU A 325     1066   1077   1435    -27    -10    -23       N  
ATOM   2528  CA  LEU A 325      23.889  31.195  56.025  1.00  9.77           C  
ANISOU 2528  CA  LEU A 325     1111   1120   1480    -43    -15    -37       C  
ATOM   2529  C   LEU A 325      22.883  30.055  56.010  1.00 10.18           C  
ANISOU 2529  C   LEU A 325     1160   1161   1546    -58    -15    -34       C  
ATOM   2530  O   LEU A 325      21.927  30.089  55.220  1.00 11.11           O  
ANISOU 2530  O   LEU A 325     1272   1286   1662    -73    -21    -40       O  
ATOM   2531  CB  LEU A 325      25.058  30.852  55.104  1.00 10.17           C  
ANISOU 2531  CB  LEU A 325     1173   1161   1530    -42    -15    -54       C  
ATOM   2532  CG  LEU A 325      25.862  32.084  54.607  1.00 10.17           C  
ANISOU 2532  CG  LEU A 325     1174   1174   1514    -32    -18    -60       C  
ATOM   2533  CD1 LEU A 325      27.227  31.740  54.035  1.00  9.94           C  
ANISOU 2533  CD1 LEU A 325     1154   1136   1485    -27    -14    -73       C  
ATOM   2534  CD2 LEU A 325      25.077  32.903  53.560  1.00 10.59           C  
ANISOU 2534  CD2 LEU A 325     1224   1244   1557    -42    -26    -66       C  
ATOM   2535  N   ALA A 326      23.077  29.122  56.919  1.00 10.63           N  
ANISOU 2535  N   ALA A 326     1219   1203   1615    -56     -7    -25       N  
ATOM   2536  CA  ALA A 326      22.206  27.982  57.012  1.00 10.96           C  
ANISOU 2536  CA  ALA A 326     1260   1233   1673    -71     -5    -22       C  
ATOM   2537  C   ALA A 326      20.934  28.225  57.817  1.00 10.65           C  
ANISOU 2537  C   ALA A 326     1207   1205   1635    -75     -5     -4       C  
ATOM   2538  O   ALA A 326      20.116  27.315  57.972  1.00 11.98           O  
ANISOU 2538  O   ALA A 326     1372   1365   1816    -90     -3      2       O  
ATOM   2539  CB  ALA A 326      22.978  26.816  57.586  1.00 10.79           C  
ANISOU 2539  CB  ALA A 326     1248   1187   1664    -66      4    -19       C  
ATOM   2540  N   HIS A 327      20.746  29.421  58.351  1.00 10.72           N  
ANISOU 2540  N   HIS A 327     1209   1234   1632    -63     -6      6       N  
ATOM   2541  CA  HIS A 327      19.606  29.693  59.188  1.00 10.66           C  
ANISOU 2541  CA  HIS A 327     1188   1238   1625    -64     -4     23       C  
ATOM   2542  C   HIS A 327      18.317  29.663  58.358  1.00 10.91           C  
ANISOU 2542  C   HIS A 327     1208   1279   1657    -83    -11     20       C  
ATOM   2543  O   HIS A 327      18.323  30.139  57.250  1.00 10.65           O  
ANISOU 2543  O   HIS A 327     1176   1254   1617    -88    -19      7       O  
ATOM   2544  CB  HIS A 327      19.779  31.055  59.835  1.00 10.65           C  
ANISOU 2544  CB  HIS A 327     1183   1254   1608    -46     -4     30       C  
ATOM   2545  CG  HIS A 327      18.748  31.355  60.863  1.00 10.68           C  
ANISOU 2545  CG  HIS A 327     1175   1270   1611    -43      1     49       C  
ATOM   2546  ND1 HIS A 327      17.507  31.836  60.514  1.00 10.74           N  
ANISOU 2546  ND1 HIS A 327     1170   1295   1617    -50     -3     53       N  
ATOM   2547  CD2 HIS A 327      18.750  31.244  62.216  1.00 10.65           C  
ANISOU 2547  CD2 HIS A 327     1171   1267   1609    -32      9     65       C  
ATOM   2548  CE1 HIS A 327      16.783  32.013  61.604  1.00 11.18           C  
ANISOU 2548  CE1 HIS A 327     1216   1359   1672    -44      3     71       C  
ATOM   2549  NE2 HIS A 327      17.505  31.651  62.649  1.00 10.51           N  
ANISOU 2549  NE2 HIS A 327     1140   1265   1590    -34     11     78       N  
ATOM   2550  N   PRO A 328      17.193  29.186  58.918  1.00 11.69           N  
ANISOU 2550  N   PRO A 328     1296   1381   1765    -93     -9     34       N  
ATOM   2551  CA  PRO A 328      15.930  29.136  58.171  1.00 11.79           C  
ANISOU 2551  CA  PRO A 328     1296   1406   1780   -112    -16     32       C  
ATOM   2552  C   PRO A 328      15.510  30.434  57.476  1.00 11.42           C  
ANISOU 2552  C   PRO A 328     1240   1382   1718   -107    -24     29       C  
ATOM   2553  O   PRO A 328      14.884  30.382  56.397  1.00 11.65           O  
ANISOU 2553  O   PRO A 328     1262   1418   1745   -123    -34     20       O  
ATOM   2554  CB  PRO A 328      14.946  28.736  59.245  1.00 12.37           C  
ANISOU 2554  CB  PRO A 328     1356   1482   1862   -116     -9     53       C  
ATOM   2555  CG  PRO A 328      15.731  27.821  60.113  1.00 12.65           C  
ANISOU 2555  CG  PRO A 328     1403   1495   1907   -110      1     59       C  
ATOM   2556  CD  PRO A 328      17.106  28.461  60.185  1.00 11.74           C  
ANISOU 2556  CD  PRO A 328     1301   1377   1782    -90      2     51       C  
ATOM   2557  N   TYR A 329      15.815  31.600  58.056  1.00 10.93           N  
ANISOU 2557  N   TYR A 329     1177   1331   1643    -87    -22     36       N  
ATOM   2558  CA  TYR A 329      15.435  32.825  57.392  1.00 10.34           C  
ANISOU 2558  CA  TYR A 329     1097   1277   1556    -81    -29     33       C  
ATOM   2559  C   TYR A 329      15.918  32.887  55.960  1.00 10.23           C  
ANISOU 2559  C   TYR A 329     1091   1262   1536    -90    -38     14       C  
ATOM   2560  O   TYR A 329      15.204  33.443  55.084  1.00  9.74           O  
ANISOU 2560  O   TYR A 329     1019   1215   1466    -96    -47     11       O  
ATOM   2561  CB  TYR A 329      15.940  34.024  58.188  1.00 10.29           C  
ANISOU 2561  CB  TYR A 329     1094   1279   1538    -58    -24     40       C  
ATOM   2562  CG  TYR A 329      15.478  35.403  57.642  1.00 10.29           C  
ANISOU 2562  CG  TYR A 329     1088   1298   1524    -50    -30     40       C  
ATOM   2563  CD1 TYR A 329      14.145  35.653  57.345  1.00 10.34           C  
ANISOU 2563  CD1 TYR A 329     1077   1322   1530    -56    -34     48       C  
ATOM   2564  CD2 TYR A 329      16.373  36.515  57.493  1.00 10.14           C  
ANISOU 2564  CD2 TYR A 329     1079   1280   1492    -34    -31     34       C  
ATOM   2565  CE1 TYR A 329      13.734  36.887  56.856  1.00 10.29           C  
ANISOU 2565  CE1 TYR A 329     1065   1332   1511    -47    -39     50       C  
ATOM   2566  CE2 TYR A 329      15.952  37.755  57.029  1.00 10.73           C  
ANISOU 2566  CE2 TYR A 329     1150   1371   1555    -26    -35     35       C  
ATOM   2567  CZ  TYR A 329      14.648  37.948  56.716  1.00 10.46           C  
ANISOU 2567  CZ  TYR A 329     1100   1353   1522    -31    -39     43       C  
ATOM   2568  OH  TYR A 329      14.228  39.149  56.273  1.00 11.38           O  
ANISOU 2568  OH  TYR A 329     1212   1485   1628    -22    -43     46       O  
ATOM   2569  N   LEU A 330      17.126  32.388  55.690  1.00  9.96           N  
ANISOU 2569  N   LEU A 330     1071   1209   1503    -88    -37      1       N  
ATOM   2570  CA  LEU A 330      17.765  32.496  54.397  1.00 10.51           C  
ANISOU 2570  CA  LEU A 330     1150   1277   1565    -93    -43    -18       C  
ATOM   2571  C   LEU A 330      17.528  31.345  53.423  1.00 10.68           C  
ANISOU 2571  C   LEU A 330     1175   1289   1595   -115    -48    -32       C  
ATOM   2572  O   LEU A 330      18.181  31.254  52.406  1.00 10.48           O  
ANISOU 2572  O   LEU A 330     1159   1259   1564   -119    -52    -49       O  
ATOM   2573  CB  LEU A 330      19.259  32.680  54.615  1.00 10.99           C  
ANISOU 2573  CB  LEU A 330     1226   1327   1623    -79    -38    -24       C  
ATOM   2574  CG  LEU A 330      19.580  33.962  55.423  1.00 11.88           C  
ANISOU 2574  CG  LEU A 330     1338   1451   1726    -58    -35    -14       C  
ATOM   2575  CD1 LEU A 330      21.050  34.029  55.729  1.00 12.47           C  
ANISOU 2575  CD1 LEU A 330     1426   1515   1798    -46    -30    -19       C  
ATOM   2576  CD2 LEU A 330      19.127  35.224  54.693  1.00 12.24           C  
ANISOU 2576  CD2 LEU A 330     1378   1515   1757    -55    -42    -15       C  
ATOM   2577  N   GLU A 331      16.544  30.497  53.716  1.00 11.47           N  
ANISOU 2577  N   GLU A 331     1265   1385   1706   -130    -48    -25       N  
ATOM   2578  CA  GLU A 331      16.402  29.239  53.004  1.00 12.67           C  
ANISOU 2578  CA  GLU A 331     1422   1522   1868   -152    -51    -38       C  
ATOM   2579  C   GLU A 331      16.139  29.356  51.524  1.00 12.06           C  
ANISOU 2579  C   GLU A 331     1345   1454   1782   -166    -63    -55       C  
ATOM   2580  O   GLU A 331      16.480  28.437  50.802  1.00 12.74           O  
ANISOU 2580  O   GLU A 331     1442   1525   1872   -180    -64    -72       O  
ATOM   2581  CB  GLU A 331      15.335  28.364  53.679  1.00 14.87           C  
ANISOU 2581  CB  GLU A 331     1691   1797   2163   -167    -49    -26       C  
ATOM   2582  CG  GLU A 331      13.941  28.912  53.594  1.00 18.09           C  
ANISOU 2582  CG  GLU A 331     2078   2230   2567   -175    -56    -15       C  
ATOM   2583  CD  GLU A 331      13.169  28.522  52.354  1.00 22.00           C  
ANISOU 2583  CD  GLU A 331     2567   2732   3061   -200    -68    -27       C  
ATOM   2584  OE1 GLU A 331      13.506  27.473  51.761  1.00 24.27           O  
ANISOU 2584  OE1 GLU A 331     2866   3000   3356   -216    -69    -43       O  
ATOM   2585  OE2 GLU A 331      12.218  29.277  51.997  1.00 26.77           O  
ANISOU 2585  OE2 GLU A 331     3153   3361   3656   -203    -76    -21       O  
ATOM   2586  N   GLN A 332      15.523  30.433  51.030  1.00 11.72           N  
ANISOU 2586  N   GLN A 332     1290   1436   1725   -164    -71    -52       N  
ATOM   2587  CA  GLN A 332      15.307  30.550  49.603  1.00 12.03           C  
ANISOU 2587  CA  GLN A 332     1331   1487   1754   -177    -83    -67       C  
ATOM   2588  C   GLN A 332      16.633  30.639  48.855  1.00 11.78           C  
ANISOU 2588  C   GLN A 332     1317   1445   1713   -170    -82    -85       C  
ATOM   2589  O   GLN A 332      16.720  30.222  47.710  1.00 11.90           O  
ANISOU 2589  O   GLN A 332     1339   1459   1724   -183    -88   -103       O  
ATOM   2590  CB  GLN A 332      14.445  31.802  49.276  1.00 12.43           C  
ANISOU 2590  CB  GLN A 332     1365   1567   1792   -172    -92    -57       C  
ATOM   2591  CG  GLN A 332      14.010  31.997  47.801  1.00 13.69           C  
ANISOU 2591  CG  GLN A 332     1522   1743   1938   -186   -106    -70       C  
ATOM   2592  CD  GLN A 332      13.093  30.907  47.273  1.00 15.10           C  
ANISOU 2592  CD  GLN A 332     1692   1921   2123   -214   -114    -77       C  
ATOM   2593  OE1 GLN A 332      13.567  29.837  46.899  1.00 17.53           O  
ANISOU 2593  OE1 GLN A 332     2014   2208   2437   -228   -112    -94       O  
ATOM   2594  NE2 GLN A 332      11.785  31.176  47.193  1.00 13.72           N  
ANISOU 2594  NE2 GLN A 332     1497   1768   1948   -224   -122    -66       N  
ATOM   2595  N   TYR A 333      17.654  31.236  49.500  1.00 11.01           N  
ANISOU 2595  N   TYR A 333     1228   1343   1614   -148    -73    -80       N  
ATOM   2596  CA  TYR A 333      18.885  31.582  48.799  1.00 10.98           C  
ANISOU 2596  CA  TYR A 333     1237   1335   1599   -139    -72    -94       C  
ATOM   2597  C   TYR A 333      20.045  30.639  49.153  1.00 11.29           C  
ANISOU 2597  C   TYR A 333     1292   1349   1649   -134    -62   -102       C  
ATOM   2598  O   TYR A 333      20.992  30.516  48.385  1.00 11.05           O  
ANISOU 2598  O   TYR A 333     1273   1312   1613   -132    -61   -118       O  
ATOM   2599  CB  TYR A 333      19.281  33.060  49.095  1.00 10.43           C  
ANISOU 2599  CB  TYR A 333     1166   1281   1518   -119    -71    -84       C  
ATOM   2600  CG  TYR A 333      18.105  33.965  49.007  1.00  9.78           C  
ANISOU 2600  CG  TYR A 333     1068   1220   1428   -119    -79    -72       C  
ATOM   2601  CD1 TYR A 333      17.420  34.093  47.781  1.00 10.17           C  
ANISOU 2601  CD1 TYR A 333     1111   1284   1467   -133    -90    -79       C  
ATOM   2602  CD2 TYR A 333      17.604  34.603  50.108  1.00  9.94           C  
ANISOU 2602  CD2 TYR A 333     1078   1247   1450   -107    -75    -53       C  
ATOM   2603  CE1 TYR A 333      16.286  34.874  47.680  1.00  9.98           C  
ANISOU 2603  CE1 TYR A 333     1072   1283   1437   -133    -97    -67       C  
ATOM   2604  CE2 TYR A 333      16.489  35.374  50.002  1.00  9.97           C  
ANISOU 2604  CE2 TYR A 333     1068   1272   1448   -107    -81    -42       C  
ATOM   2605  CZ  TYR A 333      15.790  35.493  48.820  1.00 10.15           C  
ANISOU 2605  CZ  TYR A 333     1084   1310   1463   -120    -92    -48       C  
ATOM   2606  OH  TYR A 333      14.592  36.217  48.711  1.00  9.99           O  
ANISOU 2606  OH  TYR A 333     1046   1311   1437   -119    -99    -35       O  
ATOM   2607  N   TYR A 334      19.964  29.980  50.311  1.00 11.33           N  
ANISOU 2607  N   TYR A 334     1296   1340   1669   -132    -54    -91       N  
ATOM   2608  CA  TYR A 334      21.082  29.200  50.800  1.00 11.66           C  
ANISOU 2608  CA  TYR A 334     1351   1360   1721   -123    -44    -95       C  
ATOM   2609  C   TYR A 334      21.450  28.075  49.820  1.00 12.44           C  
ANISOU 2609  C   TYR A 334     1462   1441   1825   -137    -44   -116       C  
ATOM   2610  O   TYR A 334      20.586  27.292  49.405  1.00 13.49           O  
ANISOU 2610  O   TYR A 334     1593   1568   1963   -157    -49   -122       O  
ATOM   2611  CB  TYR A 334      20.777  28.635  52.154  1.00 12.55           C  
ANISOU 2611  CB  TYR A 334     1459   1461   1848   -120    -37    -78       C  
ATOM   2612  CG  TYR A 334      21.871  27.811  52.782  1.00 12.45           C  
ANISOU 2612  CG  TYR A 334     1459   1426   1847   -110    -26    -79       C  
ATOM   2613  CD1 TYR A 334      23.187  28.260  52.880  1.00 12.81           C  
ANISOU 2613  CD1 TYR A 334     1512   1470   1885    -92    -22    -82       C  
ATOM   2614  CD2 TYR A 334      21.580  26.540  53.289  1.00 12.83           C  
ANISOU 2614  CD2 TYR A 334     1510   1454   1912   -119    -21    -75       C  
ATOM   2615  CE1 TYR A 334      24.163  27.487  53.494  1.00 12.41           C  
ANISOU 2615  CE1 TYR A 334     1470   1400   1845    -81    -13    -80       C  
ATOM   2616  CE2 TYR A 334      22.554  25.764  53.891  1.00 13.52           C  
ANISOU 2616  CE2 TYR A 334     1608   1520   2010   -108    -11    -73       C  
ATOM   2617  CZ  TYR A 334      23.823  26.252  54.010  1.00 13.59           C  
ANISOU 2617  CZ  TYR A 334     1622   1529   2011    -89     -7    -75       C  
ATOM   2618  OH  TYR A 334      24.813  25.556  54.648  1.00 14.12           O  
ANISOU 2618  OH  TYR A 334     1698   1579   2088    -76      2    -72       O  
ATOM   2619  N   ASP A 335      22.720  28.024  49.467  1.00 12.48           N  
ANISOU 2619  N   ASP A 335     1479   1437   1825   -126    -39   -127       N  
ATOM   2620  CA  ASP A 335      23.214  27.050  48.488  1.00 13.33           C  
ANISOU 2620  CA  ASP A 335     1600   1528   1935   -135    -37   -148       C  
ATOM   2621  C   ASP A 335      24.721  26.948  48.681  1.00 13.79           C  
ANISOU 2621  C   ASP A 335     1670   1576   1995   -115    -27   -153       C  
ATOM   2622  O   ASP A 335      25.475  27.676  48.084  1.00 12.33           O  
ANISOU 2622  O   ASP A 335     1487   1402   1797   -107    -27   -160       O  
ATOM   2623  CB  ASP A 335      22.889  27.503  47.058  1.00 14.89           C  
ANISOU 2623  CB  ASP A 335     1798   1742   2117   -146    -47   -164       C  
ATOM   2624  CG  ASP A 335      23.348  26.506  46.012  1.00 16.50           C  
ANISOU 2624  CG  ASP A 335     2017   1930   2321   -156    -45   -188       C  
ATOM   2625  OD1 ASP A 335      23.905  25.486  46.415  1.00 17.13           O  
ANISOU 2625  OD1 ASP A 335     2108   1986   2416   -153    -36   -192       O  
ATOM   2626  OD2 ASP A 335      23.183  26.858  44.825  1.00 17.52           O  
ANISOU 2626  OD2 ASP A 335     2148   2074   2435   -165    -53   -202       O  
ATOM   2627  N   PRO A 336      25.136  26.025  49.561  1.00 15.90           N  
ANISOU 2627  N   PRO A 336     1942   1821   2278   -109    -18   -146       N  
ATOM   2628  CA  PRO A 336      26.557  25.967  49.876  1.00 18.10           C  
ANISOU 2628  CA  PRO A 336     2228   2090   2558    -89     -8   -147       C  
ATOM   2629  C   PRO A 336      27.445  25.542  48.683  1.00 19.80           C  
ANISOU 2629  C   PRO A 336     2456   2298   2769    -88     -5   -170       C  
ATOM   2630  O   PRO A 336      28.635  25.839  48.700  1.00 24.28           O  
ANISOU 2630  O   PRO A 336     3026   2866   3331    -72      1   -171       O  
ATOM   2631  CB  PRO A 336      26.622  24.982  51.075  1.00 20.00           C  
ANISOU 2631  CB  PRO A 336     2472   2310   2819    -84      0   -134       C  
ATOM   2632  CG  PRO A 336      25.283  24.400  51.216  1.00 18.56           C  
ANISOU 2632  CG  PRO A 336     2285   2123   2646   -103     -4   -130       C  
ATOM   2633  CD  PRO A 336      24.310  25.144  50.395  1.00 17.56           C  
ANISOU 2633  CD  PRO A 336     2149   2016   2505   -118    -15   -135       C  
ATOM   2634  N   THR A 337      26.863  25.022  47.616  1.00 17.69           N  
ANISOU 2634  N   THR A 337     2195   2027   2499   -106     -9   -187       N  
ATOM   2635  CA  THR A 337      27.590  24.795  46.354  1.00 18.58           C  
ANISOU 2635  CA  THR A 337     2320   2138   2603   -107     -7   -210       C  
ATOM   2636  C   THR A 337      27.849  26.054  45.534  1.00 18.63           C  
ANISOU 2636  C   THR A 337     2320   2170   2587   -104    -13   -214       C  
ATOM   2637  O   THR A 337      28.569  26.024  44.506  1.00 18.79           O  
ANISOU 2637  O   THR A 337     2350   2193   2598   -102    -10   -231       O  
ATOM   2638  CB  THR A 337      26.888  23.754  45.448  1.00 19.44           C  
ANISOU 2638  CB  THR A 337     2438   2232   2715   -129    -10   -229       C  
ATOM   2639  OG1 THR A 337      25.738  24.325  44.800  1.00 20.21           O  
ANISOU 2639  OG1 THR A 337     2527   2350   2801   -147    -24   -232       O  
ATOM   2640  CG2 THR A 337      26.529  22.517  46.261  1.00 22.61           C  
ANISOU 2640  CG2 THR A 337     2845   2607   3140   -134     -4   -224       C  
ATOM   2641  N   ASP A 338      27.281  27.170  45.983  1.00 14.30           N  
ANISOU 2641  N   ASP A 338     1759   1642   2031   -103    -21   -198       N  
ATOM   2642  CA  ASP A 338      27.345  28.434  45.267  1.00 13.87           C  
ANISOU 2642  CA  ASP A 338     1700   1613   1958   -101    -27   -199       C  
ATOM   2643  C   ASP A 338      27.726  29.537  46.206  1.00 12.83           C  
ANISOU 2643  C   ASP A 338     1559   1493   1823    -85    -26   -180       C  
ATOM   2644  O   ASP A 338      27.300  30.687  46.033  1.00 12.82           O  
ANISOU 2644  O   ASP A 338     1550   1512   1810    -86    -33   -173       O  
ATOM   2645  CB  ASP A 338      25.984  28.786  44.640  1.00 14.81           C  
ANISOU 2645  CB  ASP A 338     1811   1747   2067   -120    -40   -200       C  
ATOM   2646  CG  ASP A 338      26.073  29.929  43.634  1.00 17.15           C  
ANISOU 2646  CG  ASP A 338     2105   2068   2342   -119    -47   -204       C  
ATOM   2647  OD1 ASP A 338      27.092  30.041  42.923  1.00 17.94           O  
ANISOU 2647  OD1 ASP A 338     2213   2169   2433   -113    -42   -216       O  
ATOM   2648  OD2 ASP A 338      25.084  30.683  43.511  1.00 18.60           O  
ANISOU 2648  OD2 ASP A 338     2278   2269   2518   -126    -57   -196       O  
ATOM   2649  N   GLU A 339      28.509  29.178  47.220  1.00 11.57           N  
ANISOU 2649  N   GLU A 339     1401   1320   1675    -71    -17   -172       N  
ATOM   2650  CA  GLU A 339      28.969  30.176  48.247  1.00 10.68           C  
ANISOU 2650  CA  GLU A 339     1280   1218   1560    -56    -16   -155       C  
ATOM   2651  C   GLU A 339      30.503  29.946  48.402  1.00 10.62           C  
ANISOU 2651  C   GLU A 339     1278   1202   1555    -40     -6   -158       C  
ATOM   2652  O   GLU A 339      30.950  29.263  49.340  1.00 10.39           O  
ANISOU 2652  O   GLU A 339     1250   1159   1539    -31      1   -151       O  
ATOM   2653  CB  GLU A 339      28.212  29.934  49.529  1.00 11.10           C  
ANISOU 2653  CB  GLU A 339     1327   1265   1626    -56    -16   -138       C  
ATOM   2654  CG  GLU A 339      26.766  30.391  49.374  1.00 11.07           C  
ANISOU 2654  CG  GLU A 339     1315   1274   1617    -69    -26   -132       C  
ATOM   2655  CD  GLU A 339      25.760  29.850  50.350  1.00 11.32           C  
ANISOU 2655  CD  GLU A 339     1340   1298   1661    -75    -26   -119       C  
ATOM   2656  OE1 GLU A 339      26.104  29.160  51.326  1.00 12.45           O  
ANISOU 2656  OE1 GLU A 339     1485   1427   1817    -68    -18   -111       O  
ATOM   2657  OE2 GLU A 339      24.532  30.086  50.128  1.00 12.43           O  
ANISOU 2657  OE2 GLU A 339     1473   1450   1800    -87    -33   -116       O  
ATOM   2658  N   PRO A 340      31.268  30.445  47.441  1.00 11.08           N  
ANISOU 2658  N   PRO A 340     1340   1270   1601    -38     -5   -169       N  
ATOM   2659  CA  PRO A 340      32.695  30.076  47.387  1.00 11.73           C  
ANISOU 2659  CA  PRO A 340     1427   1346   1685    -24      5   -175       C  
ATOM   2660  C   PRO A 340      33.556  30.663  48.493  1.00 11.66           C  
ANISOU 2660  C   PRO A 340     1411   1342   1679     -9      8   -159       C  
ATOM   2661  O   PRO A 340      33.161  31.626  49.181  1.00 11.25           O  
ANISOU 2661  O   PRO A 340     1352   1301   1622     -8      2   -146       O  
ATOM   2662  CB  PRO A 340      33.155  30.536  46.019  1.00 13.10           C  
ANISOU 2662  CB  PRO A 340     1604   1531   1843    -27      4   -190       C  
ATOM   2663  CG  PRO A 340      32.157  31.497  45.531  1.00 13.13           C  
ANISOU 2663  CG  PRO A 340     1604   1552   1835    -39     -6   -187       C  
ATOM   2664  CD  PRO A 340      30.871  31.279  46.308  1.00 11.70           C  
ANISOU 2664  CD  PRO A 340     1417   1366   1662    -47    -13   -177       C  
ATOM   2665  N   VAL A 341      34.675  30.008  48.700  1.00 11.44           N  
ANISOU 2665  N   VAL A 341     1385   1303   1657      4     17   -162       N  
ATOM   2666  CA  VAL A 341      35.694  30.395  49.645  1.00 11.43           C  
ANISOU 2666  CA  VAL A 341     1378   1307   1658     19     20   -149       C  
ATOM   2667  C   VAL A 341      36.981  30.793  48.941  1.00 11.82           C  
ANISOU 2667  C   VAL A 341     1427   1367   1699     27     25   -157       C  
ATOM   2668  O   VAL A 341      37.203  30.546  47.753  1.00 13.25           O  
ANISOU 2668  O   VAL A 341     1613   1547   1874     23     29   -173       O  
ATOM   2669  CB  VAL A 341      35.961  29.319  50.687  1.00 12.10           C  
ANISOU 2669  CB  VAL A 341     1464   1375   1760     29     26   -141       C  
ATOM   2670  CG1 VAL A 341      34.705  29.034  51.499  1.00 12.99           C  
ANISOU 2670  CG1 VAL A 341     1576   1480   1881     21     22   -130       C  
ATOM   2671  CG2 VAL A 341      36.556  28.040  50.045  1.00 12.70           C  
ANISOU 2671  CG2 VAL A 341     1548   1432   1845     34     36   -154       C  
ATOM   2672  N   ALA A 342      37.871  31.433  49.703  1.00 12.32           N  
ANISOU 2672  N   ALA A 342     1482   1440   1761     38     26   -146       N  
ATOM   2673  CA  ALA A 342      39.147  31.908  49.184  1.00 15.18           C  
ANISOU 2673  CA  ALA A 342     1839   1813   2114     45     31   -150       C  
ATOM   2674  C   ALA A 342      40.108  30.782  48.960  1.00 16.76           C  
ANISOU 2674  C   ALA A 342     2042   2002   2324     57     42   -157       C  
ATOM   2675  O   ALA A 342      40.042  29.825  49.651  1.00 16.22           O  
ANISOU 2675  O   ALA A 342     1977   1919   2269     64     45   -153       O  
ATOM   2676  CB  ALA A 342      39.750  32.941  50.146  1.00 14.73           C  
ANISOU 2676  CB  ALA A 342     1773   1770   2053     51     27   -136       C  
ATOM   2677  N   GLU A 343      41.051  31.035  48.063  1.00 19.64           N  
ANISOU 2677  N   GLU A 343     2405   2376   2680     60     47   -167       N  
ATOM   2678  CA  GLU A 343      42.161  30.094  47.738  1.00 24.70           C  
ANISOU 2678  CA  GLU A 343     3047   3010   3327     74     60   -174       C  
ATOM   2679  C   GLU A 343      42.973  29.718  48.988  1.00 21.64           C  
ANISOU 2679  C   GLU A 343     2651   2619   2951     91     63   -159       C  
ATOM   2680  O   GLU A 343      43.244  28.555  49.247  1.00 24.18           O  
ANISOU 2680  O   GLU A 343     2976   2924   3287    102     71   -159       O  
ATOM   2681  CB  GLU A 343      43.105  30.748  46.687  1.00 28.33           C  
ANISOU 2681  CB  GLU A 343     3504   3487   3774     75     65   -182       C  
ATOM   2682  CG  GLU A 343      42.491  31.060  45.314  1.00 33.73           C  
ANISOU 2682  CG  GLU A 343     4196   4177   4445     61     63   -198       C  
ATOM   2683  CD  GLU A 343      42.016  29.821  44.577  1.00 40.83           C  
ANISOU 2683  CD  GLU A 343     5108   5057   5348     60     69   -214       C  
ATOM   2684  OE1 GLU A 343      42.832  28.917  44.370  1.00 49.10           O  
ANISOU 2684  OE1 GLU A 343     6159   6095   6403     72     80   -222       O  
ATOM   2685  OE2 GLU A 343      40.813  29.753  44.197  1.00 51.33           O  
ANISOU 2685  OE2 GLU A 343     6446   6382   6675     45     62   -221       O  
ATOM   2686  N   GLU A 344      43.265  30.714  49.816  1.00 19.89           N  
ANISOU 2686  N   GLU A 344     2419   2413   2725     91     56   -145       N  
ATOM   2687  CA  GLU A 344      44.214  30.547  50.897  1.00 17.81           C  
ANISOU 2687  CA  GLU A 344     2145   2153   2469    106     58   -131       C  
ATOM   2688  C   GLU A 344      44.048  31.686  51.933  1.00 15.67           C  
ANISOU 2688  C   GLU A 344     1867   1896   2192    101     47   -117       C  
ATOM   2689  O   GLU A 344      43.793  32.826  51.541  1.00 16.44           O  
ANISOU 2689  O   GLU A 344     1963   2006   2276     89     41   -119       O  
ATOM   2690  CB  GLU A 344      45.610  30.662  50.283  1.00 17.66           C  
ANISOU 2690  CB  GLU A 344     2117   2146   2445    116     66   -136       C  
ATOM   2691  CG  GLU A 344      46.768  30.354  51.228  1.00 16.24           C  
ANISOU 2691  CG  GLU A 344     1926   1972   2274    133     69   -122       C  
ATOM   2692  CD  GLU A 344      48.091  30.203  50.510  1.00 15.72           C  
ANISOU 2692  CD  GLU A 344     1852   1916   2206    144     80   -128       C  
ATOM   2693  OE1 GLU A 344      48.108  29.559  49.463  1.00 16.89           O  
ANISOU 2693  OE1 GLU A 344     2008   2055   2355    147     89   -143       O  
ATOM   2694  OE2 GLU A 344      49.119  30.622  51.061  1.00 13.42           O  
ANISOU 2694  OE2 GLU A 344     1545   1640   1913    152     79   -118       O  
ATOM   2695  N   PRO A 345      44.356  31.388  53.219  1.00 14.49           N  
ANISOU 2695  N   PRO A 345     1710   1745   2049    112     45   -102       N  
ATOM   2696  CA  PRO A 345      44.330  32.532  54.101  1.00 14.09           C  
ANISOU 2696  CA  PRO A 345     1653   1710   1990    107     35    -91       C  
ATOM   2697  C   PRO A 345      45.456  33.508  53.867  1.00 12.44           C  
ANISOU 2697  C   PRO A 345     1434   1521   1771    106     34    -91       C  
ATOM   2698  O   PRO A 345      46.484  33.171  53.277  1.00 11.17           O  
ANISOU 2698  O   PRO A 345     1267   1365   1612    114     42    -95       O  
ATOM   2699  CB  PRO A 345      44.484  31.923  55.494  1.00 15.33           C  
ANISOU 2699  CB  PRO A 345     1806   1863   2157    119     34    -75       C  
ATOM   2700  CG  PRO A 345      44.034  30.517  55.345  1.00 17.55           C  
ANISOU 2700  CG  PRO A 345     2095   2121   2451    125     42    -78       C  
ATOM   2701  CD  PRO A 345      44.573  30.138  53.958  1.00 16.48           C  
ANISOU 2701  CD  PRO A 345     1963   1982   2316    126     51    -94       C  
ATOM   2702  N   PHE A 346      45.295  34.703  54.394  1.00 10.70           N  
ANISOU 2702  N   PHE A 346     1211   1314   1542     97     25    -85       N  
ATOM   2703  CA  PHE A 346      46.285  35.770  54.322  1.00 11.00           C  
ANISOU 2703  CA  PHE A 346     1238   1370   1569     94     22    -83       C  
ATOM   2704  C   PHE A 346      46.986  35.974  55.665  1.00 10.82           C  
ANISOU 2704  C   PHE A 346     1206   1359   1548    100     17    -70       C  
ATOM   2705  O   PHE A 346      46.466  35.590  56.710  1.00 11.09           O  
ANISOU 2705  O   PHE A 346     1242   1386   1585    105     13    -61       O  
ATOM   2706  CB  PHE A 346      45.666  37.118  53.901  1.00 11.28           C  
ANISOU 2706  CB  PHE A 346     1280   1413   1593     78     16    -87       C  
ATOM   2707  CG  PHE A 346      45.035  37.133  52.514  1.00 11.65           C  
ANISOU 2707  CG  PHE A 346     1336   1454   1636     69     19   -100       C  
ATOM   2708  CD1 PHE A 346      45.371  36.197  51.535  1.00 12.75           C  
ANISOU 2708  CD1 PHE A 346     1477   1589   1780     75     29   -109       C  
ATOM   2709  CD2 PHE A 346      44.147  38.139  52.183  1.00 11.59           C  
ANISOU 2709  CD2 PHE A 346     1335   1449   1619     57     13   -101       C  
ATOM   2710  CE1 PHE A 346      44.771  36.254  50.288  1.00 13.56           C  
ANISOU 2710  CE1 PHE A 346     1588   1688   1877     66     31   -121       C  
ATOM   2711  CE2 PHE A 346      43.591  38.239  50.899  1.00 12.15           C  
ANISOU 2711  CE2 PHE A 346     1413   1518   1685     49     16   -112       C  
ATOM   2712  CZ  PHE A 346      43.890  37.259  49.974  1.00 12.38           C  
ANISOU 2712  CZ  PHE A 346     1444   1542   1718     53     24   -122       C  
ATOM   2713  N   THR A 347      48.152  36.591  55.619  1.00 10.55           N  
ANISOU 2713  N   THR A 347     1160   1341   1507    100     16    -68       N  
ATOM   2714  CA  THR A 347      48.868  37.005  56.812  1.00 11.77           C  
ANISOU 2714  CA  THR A 347     1304   1510   1660    103      9    -57       C  
ATOM   2715  C   THR A 347      49.295  38.435  56.673  1.00 12.11           C  
ANISOU 2715  C   THR A 347     1343   1568   1690     88      2    -59       C  
ATOM   2716  O   THR A 347      49.751  38.890  55.613  1.00 12.04           O  
ANISOU 2716  O   THR A 347     1332   1565   1677     82      6    -66       O  
ATOM   2717  CB  THR A 347      50.029  36.062  57.102  1.00 12.98           C  
ANISOU 2717  CB  THR A 347     1444   1668   1820    119     14    -50       C  
ATOM   2718  OG1 THR A 347      50.599  36.428  58.378  1.00 14.27           O  
ANISOU 2718  OG1 THR A 347     1597   1846   1980    122      5    -38       O  
ATOM   2719  CG2 THR A 347      51.075  36.176  55.995  1.00 13.83           C  
ANISOU 2719  CG2 THR A 347     1543   1787   1927    120     21    -57       C  
ATOM   2720  N   PHE A 348      49.142  39.202  57.758  1.00 11.89           N  
ANISOU 2720  N   PHE A 348     1315   1546   1656     83     -8    -52       N  
ATOM   2721  CA  PHE A 348      49.653  40.569  57.903  1.00 12.95           C  
ANISOU 2721  CA  PHE A 348     1446   1695   1779     69    -15    -52       C  
ATOM   2722  C   PHE A 348      50.241  40.629  59.303  1.00 15.32           C  
ANISOU 2722  C   PHE A 348     1737   2006   2077     73    -23    -42       C  
ATOM   2723  O   PHE A 348      49.494  40.545  60.314  1.00 16.72           O  
ANISOU 2723  O   PHE A 348     1921   2178   2253     76    -29    -37       O  
ATOM   2724  CB  PHE A 348      48.549  41.610  57.804  1.00 13.06           C  
ANISOU 2724  CB  PHE A 348     1475   1702   1786     55    -20    -57       C  
ATOM   2725  CG  PHE A 348      47.931  41.731  56.461  1.00 11.53           C  
ANISOU 2725  CG  PHE A 348     1290   1500   1592     50    -14    -66       C  
ATOM   2726  CD1 PHE A 348      48.650  42.228  55.400  1.00 11.95           C  
ANISOU 2726  CD1 PHE A 348     1339   1561   1642     42    -10    -71       C  
ATOM   2727  CD2 PHE A 348      46.592  41.418  56.271  1.00 11.57           C  
ANISOU 2727  CD2 PHE A 348     1308   1490   1599     50    -13    -68       C  
ATOM   2728  CE1 PHE A 348      48.058  42.341  54.146  1.00 11.20           C  
ANISOU 2728  CE1 PHE A 348     1252   1459   1544     37     -5    -79       C  
ATOM   2729  CE2 PHE A 348      46.009  41.516  55.046  1.00 11.08           C  
ANISOU 2729  CE2 PHE A 348     1253   1422   1536     45     -8    -76       C  
ATOM   2730  CZ  PHE A 348      46.753  42.013  53.986  1.00 11.41           C  
ANISOU 2730  CZ  PHE A 348     1290   1471   1572     38     -5    -82       C  
ATOM   2731  N   ALA A 349      51.532  40.787  59.397  1.00 15.28           N  
ANISOU 2731  N   ALA A 349     1716   2018   2070     73    -25    -38       N  
ATOM   2732  CA  ALA A 349      52.201  40.848  60.702  1.00 17.05           C  
ANISOU 2732  CA  ALA A 349     1930   2257   2291     76    -34    -29       C  
ATOM   2733  C   ALA A 349      51.980  42.200  61.371  1.00 18.22           C  
ANISOU 2733  C   ALA A 349     2085   2412   2427     59    -45    -30       C  
ATOM   2734  O   ALA A 349      51.894  43.199  60.701  1.00 15.44           O  
ANISOU 2734  O   ALA A 349     1739   2059   2070     45    -45    -38       O  
ATOM   2735  CB  ALA A 349      53.689  40.632  60.496  1.00 18.08           C  
ANISOU 2735  CB  ALA A 349     2039   2406   2423     80    -32    -25       C  
ATOM   2736  N   MET A 350      51.907  42.205  62.711  1.00 25.26           N  
ANISOU 2736  N   MET A 350     3892   2934   2772  -1081   -556    163       N  
ATOM   2737  CA AMET A 350      51.732  43.464  63.435  0.50 26.19           C  
ANISOU 2737  CA AMET A 350     3866   3171   2913  -1065   -496    137       C  
ATOM   2738  CA BMET A 350      51.812  43.424  63.528  0.50 26.71           C  
ANISOU 2738  CA BMET A 350     3944   3225   2979  -1066   -504    140       C  
ATOM   2739  C   MET A 350      52.872  44.438  63.135  1.00 25.80           C  
ANISOU 2739  C   MET A 350     3710   3072   3019   -874   -487    126       C  
ATOM   2740  O   MET A 350      52.654  45.660  63.150  1.00 23.84           O  
ANISOU 2740  O   MET A 350     3328   2922   2808   -822   -419     96       O  
ATOM   2741  CB AMET A 350      51.594  43.245  64.957  0.50 27.82           C  
ANISOU 2741  CB AMET A 350     4170   3381   3019  -1203   -544    156       C  
ATOM   2742  CB BMET A 350      52.029  43.072  65.017  0.50 29.40           C  
ANISOU 2742  CB BMET A 350     4410   3517   3244  -1173   -578    167       C  
ATOM   2743  CG AMET A 350      50.215  42.803  65.432  0.50 29.67           C  
ANISOU 2743  CG AMET A 350     4439   3758   3077  -1425   -511    149       C  
ATOM   2744  CG BMET A 350      50.942  42.237  65.676  0.50 31.96           C  
ANISOU 2744  CG BMET A 350     4853   3905   3384  -1409   -590    181       C  
ATOM   2745  SD AMET A 350      48.812  43.892  65.046  0.50 29.85           S  
ANISOU 2745  SD AMET A 350     4227   4062   3055  -1439   -372     79       S  
ATOM   2746  SD BMET A 350      51.398  41.690  67.345  0.50 35.90           S  
ANISOU 2746  SD BMET A 350     5545   4301   3793  -1533   -699    222       S  
ATOM   2747  CE AMET A 350      49.297  45.404  65.879  0.50 29.62           C  
ANISOU 2747  CE AMET A 350     4077   4069   3108  -1302   -342     45       C  
ATOM   2748  CE BMET A 350      52.451  40.282  66.982  0.50 35.71           C  
ANISOU 2748  CE BMET A 350     5770   4011   3786  -1470   -851    270       C  
ATOM   2749  N   GLU A 351      54.058  43.922  62.834  1.00 24.96           N  
ANISOU 2749  N   GLU A 351     3666   2827   2990   -769   -558    144       N  
ATOM   2750  CA  GLU A 351      55.208  44.790  62.559  1.00 25.97           C  
ANISOU 2750  CA  GLU A 351     3686   2933   3250   -615   -552    132       C  
ATOM   2751  C   GLU A 351      55.037  45.662  61.279  1.00 22.39           C  
ANISOU 2751  C   GLU A 351     3089   2552   2866   -531   -458    103       C  
ATOM   2752  O   GLU A 351      55.640  46.721  61.149  1.00 22.67           O  
ANISOU 2752  O   GLU A 351     3026   2611   2978   -454   -429     91       O  
ATOM   2753  CB  GLU A 351      56.476  43.949  62.500  1.00 29.82           C  
ANISOU 2753  CB  GLU A 351     4255   3289   3786   -517   -652    145       C  
ATOM   2754  CG  GLU A 351      56.867  43.303  63.851  1.00 34.60           C  
ANISOU 2754  CG  GLU A 351     5005   3807   4334   -570   -763    173       C  
ATOM   2755  CD  GLU A 351      56.137  41.985  64.160  1.00 38.77           C  
ANISOU 2755  CD  GLU A 351     5742   4260   4730   -700   -828    199       C  
ATOM   2756  OE1 GLU A 351      55.187  41.611  63.443  1.00 35.07           O  
ANISOU 2756  OE1 GLU A 351     5294   3829   4203   -776   -778    196       O  
ATOM   2757  OE2 GLU A 351      56.521  41.310  65.144  1.00 44.54           O  
ANISOU 2757  OE2 GLU A 351     6629   4890   5403   -737   -937    224       O  
ATOM   2758  N   LEU A 352      54.108  45.288  60.403  1.00 19.68           N  
ANISOU 2758  N   LEU A 352     2745   2252   2478   -569   -413     94       N  
ATOM   2759  CA  LEU A 352      53.711  46.191  59.311  1.00 19.73           C  
ANISOU 2759  CA  LEU A 352     2630   2338   2528   -508   -327     65       C  
ATOM   2760  C   LEU A 352      53.217  47.508  59.834  1.00 19.70           C  
ANISOU 2760  C   LEU A 352     2538   2433   2514   -508   -278     41       C  
ATOM   2761  O   LEU A 352      53.455  48.534  59.221  1.00 20.05           O  
ANISOU 2761  O   LEU A 352     2505   2495   2617   -424   -238     23       O  
ATOM   2762  CB  LEU A 352      52.596  45.577  58.468  1.00 19.65           C  
ANISOU 2762  CB  LEU A 352     2635   2380   2449   -570   -291     57       C  
ATOM   2763  CG  LEU A 352      52.927  44.459  57.512  1.00 21.24           C  
ANISOU 2763  CG  LEU A 352     2919   2490   2661   -547   -322     70       C  
ATOM   2764  CD1 LEU A 352      51.609  44.072  56.853  1.00 21.79           C  
ANISOU 2764  CD1 LEU A 352     2993   2643   2643   -642   -279     62       C  
ATOM   2765  CD2 LEU A 352      53.922  44.909  56.435  1.00 21.50           C  
ANISOU 2765  CD2 LEU A 352     2879   2483   2808   -401   -299     57       C  
ATOM   2766  N   ASP A 353      52.554  47.481  60.999  1.00 20.95           N  
ANISOU 2766  N   ASP A 353     2725   2650   2586   -604   -287     38       N  
ATOM   2767  CA  ASP A 353      51.950  48.663  61.590  1.00 22.13           C  
ANISOU 2767  CA  ASP A 353     2802   2904   2701   -596   -245      3       C  
ATOM   2768  C   ASP A 353      52.983  49.623  62.133  1.00 22.40           C  
ANISOU 2768  C   ASP A 353     2827   2875   2808   -525   -267      9       C  
ATOM   2769  O   ASP A 353      52.659  50.755  62.442  1.00 23.91           O  
ANISOU 2769  O   ASP A 353     2977   3124   2984   -487   -239    -22       O  
ATOM   2770  CB  ASP A 353      51.002  48.267  62.734  1.00 23.32           C  
ANISOU 2770  CB  ASP A 353     2984   3153   2725   -731   -247     -7       C  
ATOM   2771  CG  ASP A 353      49.799  47.410  62.268  1.00 26.64           C  
ANISOU 2771  CG  ASP A 353     3402   3679   3042   -840   -218    -18       C  
ATOM   2772  OD1 ASP A 353      49.699  47.050  61.077  1.00 30.18           O  
ANISOU 2772  OD1 ASP A 353     3839   4108   3520   -807   -203    -15       O  
ATOM   2773  OD2 ASP A 353      48.982  47.090  63.155  1.00 30.14           O  
ANISOU 2773  OD2 ASP A 353     3859   4231   3362   -974   -213    -30       O  
ATOM   2774  N   ASP A 354      54.226  49.198  62.223  1.00 21.06           N  
ANISOU 2774  N   ASP A 354     2699   2595   2709   -501   -323     44       N  
ATOM   2775  CA  ASP A 354      55.264  50.070  62.743  1.00 23.41           C  
ANISOU 2775  CA  ASP A 354     2980   2848   3066   -455   -349     51       C  
ATOM   2776  C   ASP A 354      56.191  50.541  61.639  1.00 20.88           C  
ANISOU 2776  C   ASP A 354     2604   2494   2837   -369   -335     52       C  
ATOM   2777  O   ASP A 354      57.106  51.295  61.918  1.00 20.84           O  
ANISOU 2777  O   ASP A 354     2579   2465   2875   -348   -354     59       O  
ATOM   2778  CB  ASP A 354      56.072  49.357  63.833  1.00 27.45           C  
ANISOU 2778  CB  ASP A 354     3565   3287   3577   -496   -433     84       C  
ATOM   2779  CG  ASP A 354      55.199  48.867  65.000  1.00 31.64           C  
ANISOU 2779  CG  ASP A 354     4171   3850   4000   -610   -450     88       C  
ATOM   2780  OD1 ASP A 354      54.239  49.583  65.372  1.00 37.90           O  
ANISOU 2780  OD1 ASP A 354     4930   4741   4730   -643   -398     57       O  
ATOM   2781  OD2 ASP A 354      55.474  47.744  65.532  1.00 36.21           O  
ANISOU 2781  OD2 ASP A 354     4851   4359   4547   -665   -522    117       O  
ATOM   2782  N   LEU A 355      55.953  50.116  60.391  1.00 19.44           N  
ANISOU 2782  N   LEU A 355     2397   2317   2674   -335   -301     45       N  
ATOM   2783  CA  LEU A 355      56.831  50.546  59.289  1.00 18.22           C  
ANISOU 2783  CA  LEU A 355     2186   2144   2592   -268   -280     42       C  
ATOM   2784  C   LEU A 355      56.719  52.049  59.093  1.00 17.22           C  
ANISOU 2784  C   LEU A 355     2035   2044   2466   -253   -243     26       C  
ATOM   2785  O   LEU A 355      55.624  52.635  59.188  1.00 17.47           O  
ANISOU 2785  O   LEU A 355     2077   2118   2441   -252   -213      3       O  
ATOM   2786  CB  LEU A 355      56.521  49.826  57.987  1.00 18.02           C  
ANISOU 2786  CB  LEU A 355     2150   2119   2577   -238   -248     34       C  
ATOM   2787  CG  LEU A 355      56.961  48.408  57.776  1.00 20.06           C  
ANISOU 2787  CG  LEU A 355     2451   2325   2846   -222   -293     44       C  
ATOM   2788  CD1 LEU A 355      56.420  47.912  56.437  1.00 20.49           C  
ANISOU 2788  CD1 LEU A 355     2505   2387   2895   -201   -250     32       C  
ATOM   2789  CD2 LEU A 355      58.477  48.338  57.827  1.00 21.83           C  
ANISOU 2789  CD2 LEU A 355     2637   2521   3135   -159   -336     45       C  
ATOM   2790  N   PRO A 356      57.852  52.716  58.839  1.00 16.99           N  
ANISOU 2790  N   PRO A 356     1976   1995   2483   -242   -250     34       N  
ATOM   2791  CA  PRO A 356      57.718  54.119  58.494  1.00 16.24           C  
ANISOU 2791  CA  PRO A 356     1898   1903   2370   -239   -223     23       C  
ATOM   2792  C   PRO A 356      56.881  54.345  57.240  1.00 14.72           C  
ANISOU 2792  C   PRO A 356     1705   1726   2160   -200   -173      2       C  
ATOM   2793  O   PRO A 356      56.859  53.501  56.314  1.00 13.15           O  
ANISOU 2793  O   PRO A 356     1473   1537   1988   -182   -150      2       O  
ATOM   2794  CB  PRO A 356      59.154  54.597  58.257  1.00 18.45           C  
ANISOU 2794  CB  PRO A 356     2145   2174   2691   -266   -238     39       C  
ATOM   2795  CG  PRO A 356      60.050  53.470  58.632  1.00 19.80           C  
ANISOU 2795  CG  PRO A 356     2262   2353   2907   -259   -277     50       C  
ATOM   2796  CD  PRO A 356      59.253  52.247  58.736  1.00 17.89           C  
ANISOU 2796  CD  PRO A 356     2045   2099   2655   -231   -284     47       C  
ATOM   2797  N   LYS A 357      56.313  55.526  57.124  1.00 13.28           N  
ANISOU 2797  N   LYS A 357     1573   1539   1932   -179   -164    -17       N  
ATOM   2798  CA  LYS A 357      55.413  55.751  56.021  1.00 13.18           C  
ANISOU 2798  CA  LYS A 357     1569   1544   1894   -128   -130    -41       C  
ATOM   2799  C   LYS A 357      56.122  55.607  54.651  1.00 12.41           C  
ANISOU 2799  C   LYS A 357     1449   1427   1840   -138   -102    -27       C  
ATOM   2800  O   LYS A 357      55.484  55.183  53.685  1.00 12.38           O  
ANISOU 2800  O   LYS A 357     1429   1443   1833   -106    -72    -39       O  
ATOM   2801  CB  LYS A 357      54.683  57.067  56.134  1.00 14.28           C  
ANISOU 2801  CB  LYS A 357     1786   1674   1966    -76   -142    -73       C  
ATOM   2802  CG  LYS A 357      55.509  58.317  56.081  1.00 15.52           C  
ANISOU 2802  CG  LYS A 357     2034   1754   2110   -101   -170    -61       C  
ATOM   2803  CD  LYS A 357      54.580  59.520  56.343  1.00 17.52           C  
ANISOU 2803  CD  LYS A 357     2395   1985   2277    -19   -201   -103       C  
ATOM   2804  CE  LYS A 357      55.322  60.840  56.153  1.00 19.65           C  
ANISOU 2804  CE  LYS A 357     2805   2152   2509    -54   -241    -89       C  
ATOM   2805  NZ  LYS A 357      56.359  60.969  57.211  1.00 20.96           N  
ANISOU 2805  NZ  LYS A 357     2979   2293   2692   -147   -267    -56       N  
ATOM   2806  N   GLU A 358      57.423  55.922  54.540  1.00 12.78           N  
ANISOU 2806  N   GLU A 358     1486   1451   1919   -188   -110     -6       N  
ATOM   2807  CA AGLU A 358      58.053  55.805  53.232  0.60 12.74           C  
ANISOU 2807  CA AGLU A 358     1448   1453   1939   -204    -76     -2       C  
ATOM   2808  CA BGLU A 358      58.151  55.771  53.262  0.40 13.21           C  
ANISOU 2808  CA BGLU A 358     1502   1514   2001   -208    -77      0       C  
ATOM   2809  C   GLU A 358      58.212  54.317  52.840  1.00 12.84           C  
ANISOU 2809  C   GLU A 358     1381   1498   2000   -174    -58     -4       C  
ATOM   2810  O   GLU A 358      58.218  54.000  51.645  1.00 12.66           O  
ANISOU 2810  O   GLU A 358     1339   1486   1986   -160    -21    -12       O  
ATOM   2811  CB AGLU A 358      59.371  56.602  53.162  0.60 13.55           C  
ANISOU 2811  CB AGLU A 358     1550   1557   2040   -286    -84     14       C  
ATOM   2812  CB BGLU A 358      59.587  56.320  53.371  0.40 14.40           C  
ANISOU 2812  CB BGLU A 358     1631   1677   2162   -286    -88     16       C  
ATOM   2813  CG AGLU A 358      60.483  56.155  54.093  0.60 13.83           C  
ANISOU 2813  CG AGLU A 358     1511   1631   2113   -321   -114     26       C  
ATOM   2814  CG BGLU A 358      60.476  55.634  54.400  0.40 15.23           C  
ANISOU 2814  CG BGLU A 358     1662   1816   2309   -298   -122     25       C  
ATOM   2815  CD AGLU A 358      60.333  56.620  55.561  0.60 13.79           C  
ANISOU 2815  CD AGLU A 358     1559   1593   2087   -337   -164     37       C  
ATOM   2816  CD BGLU A 358      61.295  54.501  53.827  0.40 15.94           C  
ANISOU 2816  CD BGLU A 358     1644   1965   2449   -269   -108     14       C  
ATOM   2817  OE1AGLU A 358      59.304  57.247  55.998  0.60 13.39           O  
ANISOU 2817  OE1AGLU A 358     1600   1497   1989   -309   -175     28       O  
ATOM   2818  OE1BGLU A 358      61.228  54.255  52.593  0.40 16.10           O  
ANISOU 2818  OE1BGLU A 358     1641   2003   2472   -251    -63      1       O  
ATOM   2819  OE2AGLU A 358      61.304  56.359  56.310  0.60 14.33           O  
ANISOU 2819  OE2AGLU A 358     1573   1692   2180   -371   -197     48       O  
ATOM   2820  OE2BGLU A 358      62.009  53.851  54.619  0.40 17.29           O  
ANISOU 2820  OE2BGLU A 358     1758   2161   2648   -253   -149     15       O  
ATOM   2821  N   ARG A 359      58.322  53.431  53.816  1.00 12.97           N  
ANISOU 2821  N   ARG A 359     1373   1518   2035   -165    -91      2       N  
ATOM   2822  CA  ARG A 359      58.351  52.020  53.509  1.00 13.57           C  
ANISOU 2822  CA  ARG A 359     1421   1599   2137   -130    -93     -2       C  
ATOM   2823  C   ARG A 359      56.990  51.525  53.063  1.00 12.33           C  
ANISOU 2823  C   ARG A 359     1300   1440   1945   -115    -71    -10       C  
ATOM   2824  O   ARG A 359      56.884  50.723  52.135  1.00 11.52           O  
ANISOU 2824  O   ARG A 359     1192   1336   1850    -92    -51    -17       O  
ATOM   2825  CB  ARG A 359      58.831  51.156  54.686  1.00 16.64           C  
ANISOU 2825  CB  ARG A 359     1810   1974   2541   -126   -152      8       C  
ATOM   2826  CG  ARG A 359      60.329  51.305  55.020  1.00 20.90           C  
ANISOU 2826  CG  ARG A 359     2285   2537   3118   -124   -183      8       C  
ATOM   2827  CD  ARG A 359      61.214  51.212  53.778  1.00 24.29           C  
ANISOU 2827  CD  ARG A 359     2638   3018   3575    -96   -147    -13       C  
ATOM   2828  NE  ARG A 359      62.648  51.317  54.070  1.00 31.77           N  
ANISOU 2828  NE  ARG A 359     3495   4032   4546    -96   -174    -24       N  
ATOM   2829  CZ  ARG A 359      63.592  51.516  53.148  1.00 31.90           C  
ANISOU 2829  CZ  ARG A 359     3415   4135   4568    -99   -139    -49       C  
ATOM   2830  NH1 ARG A 359      64.884  51.551  53.512  1.00 32.33           N  
ANISOU 2830  NH1 ARG A 359     3366   4283   4633   -100   -168    -67       N  
ATOM   2831  NH2 ARG A 359      63.265  51.665  51.870  1.00 32.93           N  
ANISOU 2831  NH2 ARG A 359     3547   4276   4687   -106    -74    -60       N  
ATOM   2832  N   LEU A 360      55.947  52.048  53.689  1.00 11.58           N  
ANISOU 2832  N   LEU A 360     1237   1361   1802   -128    -74    -16       N  
ATOM   2833  CA  LEU A 360      54.606  51.715  53.236  1.00 11.29           C  
ANISOU 2833  CA  LEU A 360     1212   1360   1717   -121    -51    -31       C  
ATOM   2834  C   LEU A 360      54.347  52.252  51.838  1.00 11.21           C  
ANISOU 2834  C   LEU A 360     1200   1354   1707    -88    -12    -44       C  
ATOM   2835  O   LEU A 360      53.736  51.582  51.021  1.00 10.40           O  
ANISOU 2835  O   LEU A 360     1093   1269   1590    -83      8    -51       O  
ATOM   2836  CB  LEU A 360      53.616  52.225  54.216  1.00 11.93           C  
ANISOU 2836  CB  LEU A 360     1304   1491   1737   -130    -61    -49       C  
ATOM   2837  CG  LEU A 360      53.602  51.638  55.614  1.00 12.39           C  
ANISOU 2837  CG  LEU A 360     1375   1558   1773   -182    -96    -38       C  
ATOM   2838  CD1 LEU A 360      52.675  52.497  56.498  1.00 14.14           C  
ANISOU 2838  CD1 LEU A 360     1598   1848   1927   -177    -96    -68       C  
ATOM   2839  CD2 LEU A 360      53.220  50.176  55.670  1.00 14.02           C  
ANISOU 2839  CD2 LEU A 360     1602   1772   1954   -236   -108    -25       C  
ATOM   2840  N   LYS A 361      54.850  53.447  51.568  1.00 10.93           N  
ANISOU 2840  N   LYS A 361     1183   1293   1676    -78     -9    -45       N  
ATOM   2841  CA  LYS A 361      54.746  54.018  50.234  1.00 10.56           C  
ANISOU 2841  CA  LYS A 361     1159   1233   1620    -60     19    -53       C  
ATOM   2842  C   LYS A 361      55.417  53.145  49.174  1.00 10.86           C  
ANISOU 2842  C   LYS A 361     1160   1267   1698    -70     51    -46       C  
ATOM   2843  O   LYS A 361      54.876  52.929  48.134  1.00 10.43           O  
ANISOU 2843  O   LYS A 361     1115   1218   1630    -53     76    -54       O  
ATOM   2844  CB  LYS A 361      55.300  55.449  50.201  1.00 10.63           C  
ANISOU 2844  CB  LYS A 361     1229   1200   1610    -75      5    -49       C  
ATOM   2845  CG  LYS A 361      55.098  56.097  48.820  1.00 11.19           C  
ANISOU 2845  CG  LYS A 361     1356   1243   1651    -66     24    -56       C  
ATOM   2846  CD  LYS A 361      55.453  57.574  48.856  1.00 11.24           C  
ANISOU 2846  CD  LYS A 361     1472   1189   1609    -92     -8    -51       C  
ATOM   2847  CE  LYS A 361      55.072  58.224  47.526  1.00 11.16           C  
ANISOU 2847  CE  LYS A 361     1552   1139   1551    -79     -5    -58       C  
ATOM   2848  NZ  LYS A 361      55.597  59.596  47.422  1.00 11.90           N  
ANISOU 2848  NZ  LYS A 361     1788   1153   1583   -133    -42    -46       N  
ATOM   2849  N   GLU A 362      56.601  52.632  49.485  1.00 11.03           N  
ANISOU 2849  N   GLU A 362     1139   1287   1765    -88     45    -36       N  
ATOM   2850  CA AGLU A 362      57.267  51.718  48.589  0.50 11.99           C  
ANISOU 2850  CA AGLU A 362     1220   1418   1917    -72     69    -43       C  
ATOM   2851  CA BGLU A 362      57.277  51.708  48.591  0.50 11.75           C  
ANISOU 2851  CA BGLU A 362     1190   1388   1888    -72     69    -43       C  
ATOM   2852  C   GLU A 362      56.427  50.467  48.314  1.00 11.47           C  
ANISOU 2852  C   GLU A 362     1176   1342   1841    -44     67    -47       C  
ATOM   2853  O   GLU A 362      56.360  49.989  47.194  1.00 10.84           O  
ANISOU 2853  O   GLU A 362     1099   1260   1760    -27     97    -57       O  
ATOM   2854  CB AGLU A 362      58.639  51.360  49.150  0.50 13.58           C  
ANISOU 2854  CB AGLU A 362     1361   1641   2159    -70     48    -44       C  
ATOM   2855  CB BGLU A 362      58.620  51.286  49.179  0.50 12.84           C  
ANISOU 2855  CB BGLU A 362     1268   1545   2065    -68     46    -44       C  
ATOM   2856  CG AGLU A 362      59.602  52.504  48.970  0.50 16.46           C  
ANISOU 2856  CG AGLU A 362     1695   2039   2520   -126     64    -42       C  
ATOM   2857  CG BGLU A 362      59.647  52.385  49.206  0.50 14.85           C  
ANISOU 2857  CG BGLU A 362     1487   1835   2321   -121     54    -41       C  
ATOM   2858  CD AGLU A 362      60.979  52.225  49.525  0.50 18.64           C  
ANISOU 2858  CD AGLU A 362     1885   2372   2827   -128     41    -51       C  
ATOM   2859  CD BGLU A 362      60.422  52.544  47.902  0.50 16.16           C  
ANISOU 2859  CD BGLU A 362     1605   2052   2483   -143    105    -59       C  
ATOM   2860  OE1AGLU A 362      61.114  51.437  50.499  0.50 23.09           O  
ANISOU 2860  OE1AGLU A 362     2437   2923   3413    -84     -8    -50       O  
ATOM   2861  OE1BGLU A 362      60.058  51.913  46.869  0.50 17.08           O  
ANISOU 2861  OE1BGLU A 362     1726   2165   2598   -105    138    -73       O  
ATOM   2862  OE2AGLU A 362      61.927  52.818  48.993  0.50 21.77           O  
ANISOU 2862  OE2AGLU A 362     2225   2834   3212   -182     69    -60       O  
ATOM   2863  OE2BGLU A 362      61.427  53.280  47.942  0.50 18.15           O  
ANISOU 2863  OE2BGLU A 362     1815   2358   2725   -210    112    -59       O  
ATOM   2864  N   LEU A 363      55.805  49.915  49.356  1.00 10.72           N  
ANISOU 2864  N   LEU A 363     1105   1241   1727    -55     30    -39       N  
ATOM   2865  CA  LEU A 363      54.900  48.761  49.159  1.00 10.39           C  
ANISOU 2865  CA  LEU A 363     1105   1193   1649    -65     23    -39       C  
ATOM   2866  C   LEU A 363      53.701  49.091  48.292  1.00 10.27           C  
ANISOU 2866  C   LEU A 363     1096   1214   1590    -74     56    -49       C  
ATOM   2867  O   LEU A 363      53.297  48.277  47.499  1.00 10.12           O  
ANISOU 2867  O   LEU A 363     1103   1190   1553    -80     67    -51       O  
ATOM   2868  CB  LEU A 363      54.482  48.149  50.498  1.00 10.53           C  
ANISOU 2868  CB  LEU A 363     1159   1208   1634   -107    -25    -26       C  
ATOM   2869  CG  LEU A 363      55.613  47.503  51.286  1.00 11.12           C  
ANISOU 2869  CG  LEU A 363     1251   1233   1743    -86    -77    -17       C  
ATOM   2870  CD1 LEU A 363      55.192  47.138  52.710  1.00 11.57           C  
ANISOU 2870  CD1 LEU A 363     1357   1282   1757   -144   -127     -1       C  
ATOM   2871  CD2 LEU A 363      56.080  46.248  50.592  1.00 12.72           C  
ANISOU 2871  CD2 LEU A 363     1500   1383   1951    -43    -97    -25       C  
ATOM   2872  N   ILE A 364      53.130  50.269  48.473  1.00  9.91           N  
ANISOU 2872  N   ILE A 364     1037   1205   1522    -68     64    -58       N  
ATOM   2873  CA  ILE A 364      51.993  50.696  47.648  1.00  9.73           C  
ANISOU 2873  CA  ILE A 364     1016   1228   1453    -52     83    -76       C  
ATOM   2874  C   ILE A 364      52.501  50.849  46.185  1.00  9.80           C  
ANISOU 2874  C   ILE A 364     1040   1198   1487    -32    115    -75       C  
ATOM   2875  O   ILE A 364      51.853  50.444  45.245  1.00 10.19           O  
ANISOU 2875  O   ILE A 364     1099   1261   1511    -31    131    -82       O  
ATOM   2876  CB  ILE A 364      51.412  52.048  48.174  1.00  9.39           C  
ANISOU 2876  CB  ILE A 364      973   1220   1374    -14     69    -97       C  
ATOM   2877  CG1 ILE A 364      50.669  51.811  49.501  1.00  9.64           C  
ANISOU 2877  CG1 ILE A 364      978   1323   1361    -37     47   -109       C  
ATOM   2878  CG2 ILE A 364      50.510  52.701  47.159  1.00  9.61           C  
ANISOU 2878  CG2 ILE A 364     1014   1279   1358     36     75   -122       C  
ATOM   2879  CD1 ILE A 364      50.413  53.041  50.360  1.00  9.69           C  
ANISOU 2879  CD1 ILE A 364      991   1353   1336     10     26   -134       C  
ATOM   2880  N   PHE A 365      53.682  51.437  45.992  1.00 10.09           N  
ANISOU 2880  N   PHE A 365     1075   1194   1563    -29    126    -68       N  
ATOM   2881  CA  PHE A 365      54.300  51.536  44.673  1.00 10.25           C  
ANISOU 2881  CA  PHE A 365     1104   1195   1597    -31    163    -70       C  
ATOM   2882  C   PHE A 365      54.473  50.134  44.033  1.00 10.35           C  
ANISOU 2882  C   PHE A 365     1106   1202   1624    -23    180    -74       C  
ATOM   2883  O   PHE A 365      54.083  49.942  42.886  1.00 10.98           O  
ANISOU 2883  O   PHE A 365     1208   1279   1684    -20    206    -81       O  
ATOM   2884  CB  PHE A 365      55.623  52.276  44.788  1.00 11.16           C  
ANISOU 2884  CB  PHE A 365     1202   1300   1737    -58    171    -65       C  
ATOM   2885  CG  PHE A 365      56.180  52.762  43.473  1.00 11.55           C  
ANISOU 2885  CG  PHE A 365     1267   1347   1773    -88    211    -69       C  
ATOM   2886  CD1 PHE A 365      55.662  53.896  42.898  1.00 12.00           C  
ANISOU 2886  CD1 PHE A 365     1404   1375   1781   -104    205    -65       C  
ATOM   2887  CD2 PHE A 365      57.282  52.177  42.875  1.00 13.38           C  
ANISOU 2887  CD2 PHE A 365     1442   1613   2029   -100    248    -81       C  
ATOM   2888  CE1 PHE A 365      56.156  54.391  41.719  1.00 12.65           C  
ANISOU 2888  CE1 PHE A 365     1523   1448   1835   -153    237    -64       C  
ATOM   2889  CE2 PHE A 365      57.783  52.665  41.645  1.00 13.43           C  
ANISOU 2889  CE2 PHE A 365     1460   1636   2007   -148    292    -88       C  
ATOM   2890  CZ  PHE A 365      57.244  53.802  41.122  1.00 13.60           C  
ANISOU 2890  CZ  PHE A 365     1576   1616   1977   -188    286    -74       C  
ATOM   2891  N   GLN A 366      54.979  49.152  44.781  1.00 10.49           N  
ANISOU 2891  N   GLN A 366     1111   1209   1667    -14    156    -72       N  
ATOM   2892  CA  GLN A 366      55.156  47.787  44.266  1.00 11.96           C  
ANISOU 2892  CA  GLN A 366     1324   1369   1853     10    154    -81       C  
ATOM   2893  C   GLN A 366      53.820  47.141  43.911  1.00 11.44           C  
ANISOU 2893  C   GLN A 366     1314   1301   1734    -21    147    -75       C  
ATOM   2894  O   GLN A 366      53.651  46.598  42.822  1.00 11.76           O  
ANISOU 2894  O   GLN A 366     1386   1325   1757    -15    168    -83       O  
ATOM   2895  CB  GLN A 366      55.789  46.916  45.337  1.00 13.96           C  
ANISOU 2895  CB  GLN A 366     1586   1595   2124     33    103    -80       C  
ATOM   2896  CG  GLN A 366      57.193  47.261  45.690  1.00 17.16           C  
ANISOU 2896  CG  GLN A 366     1923   2021   2576     71    100    -93       C  
ATOM   2897  CD  GLN A 366      58.054  47.005  44.578  1.00 20.87           C  
ANISOU 2897  CD  GLN A 366     2356   2514   3059    118    136   -124       C  
ATOM   2898  OE1 GLN A 366      58.718  47.896  44.044  1.00 26.03           O  
ANISOU 2898  OE1 GLN A 366     2943   3223   3723     99    181   -135       O  
ATOM   2899  NE2 GLN A 366      58.028  45.740  44.139  1.00 21.93           N  
ANISOU 2899  NE2 GLN A 366     2547   2607   3178    174    117   -142       N  
ATOM   2900  N   GLU A 367      52.862  47.217  44.818  1.00 11.13           N  
ANISOU 2900  N   GLU A 367     1280   1291   1657    -64    120    -64       N  
ATOM   2901  CA  GLU A 367      51.560  46.554  44.588  1.00 12.22           C  
ANISOU 2901  CA  GLU A 367     1456   1462   1727   -119    112    -62       C  
ATOM   2902  C   GLU A 367      50.819  47.106  43.399  1.00 12.52           C  
ANISOU 2902  C   GLU A 367     1478   1538   1740   -112    145    -73       C  
ATOM   2903  O   GLU A 367      50.132  46.326  42.663  1.00 13.35           O  
ANISOU 2903  O   GLU A 367     1623   1652   1799   -149    146    -72       O  
ATOM   2904  CB  GLU A 367      50.690  46.713  45.844  1.00 13.18           C  
ANISOU 2904  CB  GLU A 367     1557   1650   1800   -174     85    -58       C  
ATOM   2905  CG  GLU A 367      51.117  45.843  46.999  1.00 14.16           C  
ANISOU 2905  CG  GLU A 367     1731   1731   1918   -213     40    -41       C  
ATOM   2906  CD  GLU A 367      50.621  44.404  46.924  1.00 14.12           C  
ANISOU 2906  CD  GLU A 367     1826   1695   1843   -293      7    -27       C  
ATOM   2907  OE1 GLU A 367      49.514  44.129  46.327  1.00 15.76           O  
ANISOU 2907  OE1 GLU A 367     2041   1966   1981   -360     21    -30       O  
ATOM   2908  OE2 GLU A 367      51.240  43.525  47.535  1.00 13.61           O  
ANISOU 2908  OE2 GLU A 367     1846   1548   1775   -301    -42    -14       O  
ATOM   2909  N   THR A 368      51.023  48.387  43.130  1.00 11.17           N  
ANISOU 2909  N   THR A 368     1273   1379   1593    -68    163    -82       N  
ATOM   2910  CA  THR A 368      50.348  49.046  42.014  1.00 11.48           C  
ANISOU 2910  CA  THR A 368     1316   1442   1602    -49    181    -93       C  
ATOM   2911  C   THR A 368      51.132  48.919  40.705  1.00 11.51           C  
ANISOU 2911  C   THR A 368     1352   1389   1632    -37    216    -92       C  
ATOM   2912  O   THR A 368      50.645  49.344  39.663  1.00 11.34           O  
ANISOU 2912  O   THR A 368     1353   1374   1583    -29    228    -98       O  
ATOM   2913  CB  THR A 368      50.057  50.515  42.322  1.00 11.39           C  
ANISOU 2913  CB  THR A 368     1292   1456   1579     -4    166   -107       C  
ATOM   2914  OG1 THR A 368      51.261  51.227  42.618  1.00 10.70           O  
ANISOU 2914  OG1 THR A 368     1215   1311   1538      5    172    -97       O  
ATOM   2915  CG2 THR A 368      49.131  50.617  43.530  1.00 12.15           C  
ANISOU 2915  CG2 THR A 368     1346   1636   1634     -5    136   -121       C  
ATOM   2916  N   ALA A 369      52.358  48.395  40.727  1.00 11.42           N  
ANISOU 2916  N   ALA A 369     1340   1334   1667    -29    232    -91       N  
ATOM   2917  CA  ALA A 369      53.196  48.380  39.567  1.00 11.45           C  
ANISOU 2917  CA  ALA A 369     1352   1313   1686    -17    273   -101       C  
ATOM   2918  C   ALA A 369      52.598  47.596  38.402  1.00 12.38           C  
ANISOU 2918  C   ALA A 369     1519   1418   1767    -24    288   -106       C  
ATOM   2919  O   ALA A 369      52.790  47.936  37.257  1.00 12.26           O  
ANISOU 2919  O   ALA A 369     1521   1396   1741    -26    323   -114       O  
ATOM   2920  CB  ALA A 369      54.559  47.820  39.955  1.00 12.28           C  
ANISOU 2920  CB  ALA A 369     1424   1407   1835     12    279   -112       C  
ATOM   2921  N   ARG A 370      51.838  46.565  38.667  1.00 12.58           N  
ANISOU 2921  N   ARG A 370     1579   1440   1762    -46    259   -100       N  
ATOM   2922  CA AARG A 370      51.439  45.733  37.546  0.50 13.32           C  
ANISOU 2922  CA AARG A 370     1734   1510   1816    -61    271   -105       C  
ATOM   2923  CA BARG A 370      51.354  45.682  37.612  0.50 13.68           C  
ANISOU 2923  CA BARG A 370     1781   1557   1858    -64    267   -104       C  
ATOM   2924  C   ARG A 370      50.324  46.343  36.708  1.00 12.96           C  
ANISOU 2924  C   ARG A 370     1693   1506   1726    -87    276   -102       C  
ATOM   2925  O   ARG A 370      50.034  45.845  35.663  1.00 13.84           O  
ANISOU 2925  O   ARG A 370     1854   1601   1806   -102    289   -105       O  
ATOM   2926  CB AARG A 370      51.116  44.333  37.976  0.50 14.34           C  
ANISOU 2926  CB AARG A 370     1933   1605   1909    -92    231    -98       C  
ATOM   2927  CB BARG A 370      50.770  44.407  38.219  0.50 15.18           C  
ANISOU 2927  CB BARG A 370     2032   1730   2005   -111    222    -93       C  
ATOM   2928  CG AARG A 370      49.886  44.188  38.816  0.50 14.54           C  
ANISOU 2928  CG AARG A 370     1956   1687   1881   -169    193    -80       C  
ATOM   2929  CG BARG A 370      49.500  44.605  39.001  0.50 16.21           C  
ANISOU 2929  CG BARG A 370     2135   1938   2085   -179    192    -79       C  
ATOM   2930  CD AARG A 370      49.611  42.715  38.869  0.50 15.64           C  
ANISOU 2930  CD AARG A 370     2208   1774   1960   -228    154    -71       C  
ATOM   2931  CD BARG A 370      49.229  43.429  39.925  0.50 17.32           C  
ANISOU 2931  CD BARG A 370     2343   2060   2179   -249    145    -65       C  
ATOM   2932  NE AARG A 370      48.550  42.278  39.793  0.50 16.09           N  
ANISOU 2932  NE AARG A 370     2282   1889   1942   -340    113    -52       N  
ATOM   2933  NE BARG A 370      49.760  43.766  41.246  0.50 18.52           N  
ANISOU 2933  NE BARG A 370     2455   2213   2370   -229    126    -61       N  
ATOM   2934  CZ AARG A 370      48.725  42.138  41.111  0.50 16.46           C  
ANISOU 2934  CZ AARG A 370     2329   1935   1989   -364     80    -42       C  
ATOM   2935  CZ BARG A 370      49.490  43.142  42.383  0.50 18.49           C  
ANISOU 2935  CZ BARG A 370     2490   2211   2326   -296     82    -46       C  
ATOM   2936  NH1AARG A 370      47.744  41.685  41.895  0.50 16.54           N  
ANISOU 2936  NH1AARG A 370     2361   2011   1912   -489     47    -28       N  
ATOM   2937  NH1BARG A 370      50.057  43.608  43.502  0.50 15.86           N  
ANISOU 2937  NH1BARG A 370     2114   1878   2035   -266     69    -44       N  
ATOM   2938  NH2AARG A 370      49.900  42.454  41.639  0.50 16.90           N  
ANISOU 2938  NH2AARG A 370     2361   1935   2123   -273     80    -49       N  
ATOM   2939  NH2BARG A 370      48.632  42.107  42.418  0.50 20.02           N  
ANISOU 2939  NH2BARG A 370     2771   2411   2424   -408     50    -32       N  
ATOM   2940  N   PHE A 371      49.755  47.467  37.170  1.00 12.33           N  
ANISOU 2940  N   PHE A 371     1567   1477   1639    -78    260   -101       N  
ATOM   2941  CA  PHE A 371      48.844  48.292  36.365  1.00 12.09           C  
ANISOU 2941  CA  PHE A 371     1543   1483   1566    -67    253   -108       C  
ATOM   2942  C   PHE A 371      49.525  49.412  35.574  1.00 13.74           C  
ANISOU 2942  C   PHE A 371     1784   1646   1790    -38    274   -110       C  
ATOM   2943  O   PHE A 371      48.879  50.133  34.819  1.00 13.57           O  
ANISOU 2943  O   PHE A 371     1797   1632   1727    -20    257   -115       O  
ATOM   2944  CB  PHE A 371      47.709  48.854  37.234  1.00 11.92           C  
ANISOU 2944  CB  PHE A 371     1468   1554   1505    -52    210   -119       C  
ATOM   2945  CG  PHE A 371      46.908  47.820  37.907  1.00 12.41           C  
ANISOU 2945  CG  PHE A 371     1501   1688   1525   -115    192   -118       C  
ATOM   2946  CD1 PHE A 371      45.790  47.231  37.306  1.00 12.65           C  
ANISOU 2946  CD1 PHE A 371     1530   1793   1484   -166    179   -123       C  
ATOM   2947  CD2 PHE A 371      47.271  47.394  39.137  1.00 13.51           C  
ANISOU 2947  CD2 PHE A 371     1623   1825   1683   -142    184   -109       C  
ATOM   2948  CE1 PHE A 371      45.046  46.252  37.988  1.00 13.90           C  
ANISOU 2948  CE1 PHE A 371     1671   2030   1582   -261    160   -119       C  
ATOM   2949  CE2 PHE A 371      46.570  46.415  39.787  1.00 14.98           C  
ANISOU 2949  CE2 PHE A 371     1807   2073   1814   -227    163   -104       C  
ATOM   2950  CZ  PHE A 371      45.448  45.843  39.208  1.00 14.39           C  
ANISOU 2950  CZ  PHE A 371     1732   2078   1658   -296    152   -108       C  
ATOM   2951  N   GLN A 372      50.846  49.560  35.721  1.00 14.55           N  
ANISOU 2951  N   GLN A 372     1882   1708   1940    -41    306   -107       N  
ATOM   2952  CA  GLN A 372      51.614  50.500  34.921  1.00 16.03           C  
ANISOU 2952  CA  GLN A 372     2106   1862   2123    -55    333   -107       C  
ATOM   2953  C   GLN A 372      51.876  49.935  33.521  1.00 19.29           C  
ANISOU 2953  C   GLN A 372     2557   2256   2515    -78    377   -115       C  
ATOM   2954  O   GLN A 372      51.932  48.732  33.304  1.00 20.08           O  
ANISOU 2954  O   GLN A 372     2650   2356   2623    -74    394   -123       O  
ATOM   2955  CB  GLN A 372      52.976  50.768  35.544  1.00 15.29           C  
ANISOU 2955  CB  GLN A 372     1970   1766   2071    -71    358   -108       C  
ATOM   2956  CG  GLN A 372      52.966  51.546  36.821  1.00 14.96           C  
ANISOU 2956  CG  GLN A 372     1909   1730   2044    -60    320    -99       C  
ATOM   2957  CD  GLN A 372      52.526  52.971  36.622  1.00 14.88           C  
ANISOU 2957  CD  GLN A 372     1977   1691   1987    -60    285    -94       C  
ATOM   2958  OE1 GLN A 372      53.204  53.748  35.942  1.00 16.42           O  
ANISOU 2958  OE1 GLN A 372     2230   1853   2154   -112    301    -88       O  
ATOM   2959  NE2 GLN A 372      51.370  53.353  37.233  1.00 13.52           N  
ANISOU 2959  NE2 GLN A 372     1814   1533   1790     -3    230   -101       N  
ATOM   2960  N   PRO A 373      52.139  50.814  32.566  1.00 22.20           N  
ANISOU 2960  N   PRO A 373     2984   2602   2849   -109    394   -113       N  
ATOM   2961  CA  PRO A 373      52.098  52.263  32.686  1.00 25.03           C  
ANISOU 2961  CA  PRO A 373     3399   2933   3177   -122    361   -102       C  
ATOM   2962  C   PRO A 373      50.672  52.711  32.431  1.00 27.56           C  
ANISOU 2962  C   PRO A 373     3776   3245   3449    -72    297   -102       C  
ATOM   2963  O   PRO A 373      49.845  51.889  32.121  1.00 30.21           O  
ANISOU 2963  O   PRO A 373     4089   3612   3776    -52    292   -108       O  
ATOM   2964  CB  PRO A 373      53.003  52.711  31.544  1.00 25.28           C  
ANISOU 2964  CB  PRO A 373     3489   2945   3172   -198    409   -101       C  
ATOM   2965  CG  PRO A 373      52.786  51.653  30.531  1.00 22.80           C  
ANISOU 2965  CG  PRO A 373     3173   2641   2850   -195    446   -114       C  
ATOM   2966  CD  PRO A 373      52.767  50.394  31.303  1.00 22.94           C  
ANISOU 2966  CD  PRO A 373     3104   2689   2923   -146    451   -125       C  
ATOM   2967  N   GLY A 374      50.415  54.008  32.459  1.00 30.93           N  
ANISOU 2967  N   GLY A 374     4289   3632   3832    -52    245    -99       N  
ATOM   2968  CA  GLY A 374      49.076  54.524  32.084  1.00 38.46           C  
ANISOU 2968  CA  GLY A 374     5302   4585   4726     24    172   -111       C  
ATOM   2969  C   GLY A 374      48.952  54.846  30.589  1.00 41.74           C  
ANISOU 2969  C   GLY A 374     5834   4946   5080     -6    166   -105       C  
ATOM   2970  O   GLY A 374      48.055  54.333  29.888  1.00 47.78           O  
ANISOU 2970  O   GLY A 374     6593   5742   5820     22    151   -114       O  
TER    2971      GLY A 374                                                      
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.